{"id":58,"date":"2022-02-04T09:00:37","date_gmt":"2022-02-04T00:00:37","guid":{"rendered":"http:\/\/www.protein.osaka-u.ac.jp\/crystallography\/LabHP\/?page_id=58"},"modified":"2024-08-08T16:35:48","modified_gmt":"2024-08-08T07:35:48","slug":"publication","status":"publish","type":"page","link":"http:\/\/www.protein.osaka-u.ac.jp\/crystallography\/LabHP\/publication\/","title":{"rendered":"PUBLICATION"},"content":{"rendered":"<section>\n<h2 class=\"mt0\">Selected Publication<\/h2>\n<ul>\n<li>J.M. Schuller, J.A. Birrell, H.Tanaka, T.Konuma, H.Wulfhorst, N.Cox, S.K. Schuller, J. Thiemann, W.Lubitz, P. S\u00e9tif , T.Ikegami, B.D. Engel, G. Kurisu &amp; M.M. Nowaczyk<br \/>\nStructural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer.<br \/>\n<em>Science<\/em>\u00a0,\u00a0<strong>363<\/strong>, 257-260 (2019)<\/li>\n<li>H.Kubota-Kawai, R.Mutoh, K.Shinmura, P. S\u00e9tif, MM. Nowaczyk, M. R\u00f6gner, T. Ikegami, H. Tanaka &amp; G.Kurisu,<br \/>\nX-ray structure of an asymmetrical trimeric ferredoxin-photosystem I complex.<br \/>\n<em>Nature Plants<\/em>,\u00a0<strong>4<\/strong>, 218-224 (2018)<\/li>\n<li>A. K. Hochmal, K. Zinzius, R. Charoenwattanasatien, P. G\u00e4belein, R. Mutoh, H. Tanaka, S. Schulze, G. Liu, M. Scholz, A. Nordhues, J. N. Offenborn, G. Finazzi, C. Fufezan, K. Huang, G. Kurisu, M. Hippler.<br \/>\nCalredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast.<br \/>\n<em>Nature Commun<\/em>.,\u00a0<strong>7<\/strong>, 11847 (2016)<\/li>\n<li>T.Kon, T.Oyama, R.Shimo-Kon, K.Imamula, T.Shima, K.Sutoh &amp; G.Kurisu,<br \/>\nThe 2.8 \u00c5 crystal structure of the dynein motor domain.<br \/>\n<em>Nature<\/em>\u00a0,\u00a0<strong>484<\/strong>, 345-350 (2012)<\/li>\n<li>T. Kon, K. Sutoh and G. Kurisu.<br \/>\nX-ray structure of a functional full-length dynein motor domain.<br \/>\n<em>Nature Strut. Mol. Biol<\/em>.,\u00a0<strong>18<\/strong>, 638-642 (2011)<\/li>\n<li>N.Muraki, J.Nomata, K.Ebata, T.Mizoguchi, T.Shiba, H.Tamiaki, G.Kurisu &amp; Y.Fujita,<br \/>\nX-ray crystal structure of the light-independent protochlorophyllide reductase.<br \/>\n<em>Nature<\/em>\u00a0,\u00a0<strong>465<\/strong>, 110-114 (2010)<\/li>\n<li>G.Kurisu, H.Zhang, J.L.Smith &amp; W.A.Cramer<br \/>\nStructure of the Cytochrome\u00a0b6f\u00a0complex of Oxygenic Photosynthesis: Tuning the cavity.<br \/>\n<em>Science<\/em>,\u00a0<strong>302<\/strong>, 1009-1014 (2003)<\/li>\n<li>G.Kurisu, M.Kusunoki, E.Katoh, T.Yamazaki, K.Teshima, Y.Onda, Y.Kimata-Ariga &amp; T.Hase.<br \/>\nStructure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase.<br \/>\n<em>Nature Struct. Biol<\/em>.,\u00a0<strong>8<\/strong>, 117-121 (2001)<\/li>\n<\/ul>\n<\/section>\n<section>\n<h2>All List from Kurisu Lab<\/h2>\n<ol>\n<li>Y. Zheng, K. Sakai, K. Watanabe, H. Takagi, Y. Sato-Shiozaki, Y. Misumi, Y. Miyanoiri, G. Kurisu, T. Nogawa, R. Takita &amp; S. Takahashi. Iron-sulphur protein catalysed [4+2] cycloadditions in natural product biosynthesis. <em>Nature Commun. <\/em>(2024) <strong>15<\/strong>, 5779<\/li>\n<li>C. Jiko, J. Li, Y. Moon, Y. Tanaka, C.C. Gopalasingam, H. Shigematsu, P.S. Chae, G. Kurisu &amp; C. Gerle. NDT-C11 as a viable novel detergent for single particle cryo-EM. <em>Chempluschem.<\/em> (2024) Online ahead of print<\/li>\n<li>S. Ko, A.Toda, H. Tanaka, J. Yu &amp; G. Kurisu. Crystal structure of the stalk region of axonemal inner-arm dynein-d reveals unique features in the coiled-coil and microtubule-binding domain. <em>FEBS Lett.<\/em> (2023) <strong>597<\/strong>, 2149-2160<\/li>\n<li>C. Gerle, Y. Misumi, A. Kawamoto, H. Tanaka, H. Kubota-Kawai, R. Tokutsu, E. Kim, D. Chorev, K. Abe, C.V. Robinson, K. Mitsuoka, J. Minagawa &amp; G. Kurisu. Three structures of PSI-LHCI from Chlamydomonas reinhardtii suggest a resting state re-activated by ferredoxin. <em>Biochim Biophys Acta Bioenerg.<\/em> (2023) <strong>1864<\/strong>, 148986<\/li>\n<li>T. Yagi, A. Toda, M. Ichikawa &amp; G. Kurisu. Regulation of motor activity of ciliary outer-arm dynein by the light chain 1; Implications from the structure of the light chain bound to the microtubule-binding domain of the heavy chain. <em>Biophys Physicobiol.<\/em> (2023) <strong>20<\/strong>, e200008<\/li>\n<li>H. Kishimoto, C. Azai, T. Yamamoto, R. Mutoh, T. Nakaniwa, H. Tanaka, Y. Miyanoiri, G. Kurisu &amp; H. Oh-Oka. Soluble domains of cytochrome <em>c<\/em>-556 and Rieske iron-sulfur protein from <em>Chlorobaculum tepidu<\/em> m: Crystal structures and interaction analysis. <em>Curr Res Struct Biol.<\/em> (2023) <strong>5<\/strong>, 100101<\/li>\n<li>S. Seki, T. Nakaniwa, P. Castro-Hartmann, K. Sader, A. Kawamoto, H. Tanaka, P. Qian, G. Kurisu &amp; R. Fujii. Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 \u00c5. <em>BBA Adv. <\/em>(2022) <strong>2<\/strong>, 100064<\/li>\n<li>R. Matsumoto, S. Yoshioka, M. Yuasa, Y. Morita, G. Kurisu, &amp; N. Fujieda. An artificial metallolyase with pliable 2-His-1-carboxylate facial triad for stereoselective Michael addition. <em>Chem Sci.<\/em> (2023) <strong>14<\/strong>, 3932-3937<\/li>\n<li>T. Nakayoshi, Y. Ohnishi, H. Tanaka, G. Kurisu, H.X. Kondo &amp; Y. Takano. Effects of Active-Center Reduction of Plant-Type Ferredoxin on Its Structure and Dynamics: Computational Analysis Using Molecular Dynamics Simulations. <em>Int J Mol Sci.<\/em> (2022) <strong>23<\/strong>, 15913<\/li>\n<li>K. Yamamoto, H. Tanaka, G. Kurisu, R. Nakano, H. Yano &amp; H. Sakai. Structural insights into the substrate specificity of IMP-6 and IMP-1 metallo-\u03b2-lactamases. <em>J Biochem.<\/em> (2022) <strong>173<\/strong>, 21-30<\/li>\n<li>D. Dey, M. Nishijima, R.Tanaka, G. Kurisu, H.Tanaka &amp; H. Ito. Crystal structure and reaction mechanism of a bacterial Mg-dechelatase homolog from the Chloroflexi Anaerolineae. <em>Protein Sci.<\/em> (2022) <strong>31<\/strong>, e4430<\/li>\n<li>J. Li, N. Hamaoka, F. Makino, A. Kawamoto, Y. Lin, M. R\u00f6gner, M.M. Nowaczyk, Y.H. Lee, K. Namba, C. Gerle &amp; G Kurisu. Structure of cyanobacterial photosystem I complexed with ferredoxin at 1.97 \u00c5 resolution. <em>Commun Biol.<\/em> (2022) <strong>5<\/strong>, 951<\/li>\n<li>C. Gerle, J.I. Kishikawa, T. Yamaguchi, A. Nakanishi, O. \u00c7oruh, F. Makino, T. Miyata, A. Kawamoto, K. Yokoyama, K. Namba, G. Kurisu &amp; T. Kato. Structures of multisubunit membrane complexes with the CRYO ARM 200. <em>Microscopy (Oxf).<\/em> (2022) <strong>71<\/strong>, 249-261<\/li>\n<li>T. Kondo, R.Mutoh, S. Arai, G. Kurisu, H. Oh-Oka, S. Fujiyoshi &amp; M. Matsushita. Energy transfer fluctuation observed by single-molecule spectroscopy of red-shifted bacteriochlorophyll in the homodimeric photosynthetic reaction center. <em>J Chem Phys.<\/em> (2022) <strong>156<\/strong>, 105102<\/li>\n<li>E.H. Hemamali, L.P. Weerasinghe, H.Tanaka, G. Kurisu &amp; I.C. Perera. LcaR: a regulatory switch from Pseudomonas aeruginosa for bioengineering alkane degrading bacteria. <em>Biodegradation.<\/em> (2022) <strong>33<\/strong>, 117-133<\/li>\n<li>S.D. Zakharov, S. Savikhin, Y. Misumi, G. Kurisu, &amp; W.A. Cramer. Isothermal titration calorimetry of membrane protein interactions: FNR and the cytochrome B<sub>\u00ad\u00ad6<\/sub>f complex. <em>Biophys J. <\/em>(2022) <strong>121<\/strong>, 300-308<\/li>\n<li>G. Kurisu &amp; T. Tsukihara. Forty years of the structure of plant-type ferredoxin. <em>J Biochem. <\/em>(2022) <strong>171<\/strong>, 19-21<\/li>\n<li>L. Juniar, V. Adlfar, M. Hippler, H. Tanaka &amp; G. Kurisu. Crystallographic analysis and phasing of iron-assimilating protein 1 (FEA1) from Chlamydomonas reinhardtii.<em> Acta Crystallogr F Struct Biol Commun. <\/em>(2021) <strong>77<\/strong>, 134-139<\/li>\n<li>O. \u00c7oruh, A. Frank, H. Tanaka, A. Kawamoto, E. El-Mohsnawy, T. Kato, K. Namba, C. Gerle, M.M. Nowaczyk &amp; G. Kurisu. Cryo-EM structure of a functional monomeric Photosystem I from <em>Thermosynechococcus elongatus<\/em> reveals red chlorophyll cluster.<em> Commun. Biol. <\/em>(2021) <strong>4<\/strong>, 304<\/li>\n<li>R. Tohda, H. Tanaka, R. Mutoh, X. Zhang, Y.-H. Lee, T. Konuma, T. Ikegami, C.T. Migita &amp; G. Kurisu. Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin. <em>J. Biol. Chem. <\/em>(2021) <strong>296<\/strong>, 100217<\/li>\n<li>T. Takei, T. Ando, T. Takao, Y. Ohnishi, G. Kurisu, M. Iwaoka &amp; H. Hojo. Chemical synthesis of ferredoxin with 4 selenocysteine residues using a segment condensation method.<em> Chem Commun (Camb). <\/em>(2020) <strong>56<\/strong>, 14239-14242<\/li>\n<li>L. Juniar, H. Tanaka, K. Yoshida, T. Hisabori &amp; G. Kurisu. Structural basis for thioredoxin isoform\u2010based fine\u2010tuning of ferredoxin\u2010thioredoxin reductase activity. <em>Protein Sci. <\/em>(2020) <strong>29<\/strong>, 2538-2545<\/li>\n<li>H. Mizuno, J. Hoshino, M. So, Y. Kogure, T. Fujii, Y. Ubara, K. Takaichi, T. Nakaniwa, H. Tanaka, G. Kurisu, F. Kametani, M. Nakagawa, T. Yoshinaga, Y. Sekijima, K. Higuchi, Y. Goto &amp; M. Yazaki. Dialysis-related amyloidosis associated with a novel \u03b22-microglobulin variant. <em>Amyloid <\/em>(2020) <strong>28<\/strong>, 42-49<\/li>\n<li>N. Fujieda, K. Umakoshi, Y. Ochi, Y. Nishikawa, S. Yanagisawa, M. Kubo, G. Kurisu &amp; S. Itoh. Copper\u2013Oxygen Dynamics in the Tyrosinase Mechanism. <em>Angewandte Chemie. Intl. Edition. <\/em>(2020) <strong>59<\/strong>, 13385-13390<\/li>\n<li>H. Yamamoto, T. Mizoguchi, Y. Tsukatani, H. Tamiaki, G. Kurisu &amp; Y. Fujita. Chlorophyllide a oxidoreductase Preferentially Catalyzes 8\u2010Vinyl Reduction over B\u2010Ring Reduction of 8\u2010Vinyl Chlorophyllide a in the Late Steps of Bacteriochlorophyll Biosynthesis. <em>ChemBiochem. <\/em>(2020) <strong>11<\/strong>, 1760-1766<\/li>\n<li>Y. Ohnishi, N. Muraki, D. Kiyota, H. Okumura, S. Baba, Y. Kawano, T. Kumasaka, H. Tanaka &amp; G. Kurisu. X-ray dose-dependent structural changes of the [2Fe-2S] ferredoxin from <em>Chlamydomonas reinhardtii. J. Biochem. <\/em>(2020) <strong>167<\/strong>, 549-555<\/li>\n<li>N. Fujieda, H. Ichihashi, M. Yuasa, Y. Nishikawa, G. Kurisu &amp; S. Itoh. Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes. <em>Angewandte Chemie. Intl. Edition. <\/em>(2020) <strong>59<\/strong>, 7717-7720<\/li>\n<li>T. Kondo, R. Mutoh, H. Tabe, G. Kurisu, H. Oh-Oka, S. Fujiyoshi, M. Matsushita, Cryogenic Single-Molecule Spectroscopy of the Primary Electron Acceptor in the Photosynthetic Reaction Center. <em>J. Phys. Chem. Lett. <\/em>(2020) <strong>11<\/strong>, 3980-3986<\/li>\n<li>A. Toda, Y. Nishikawa, H. Tanaka, T. Yagi &amp; G. Kurisu, The complex of outer-arm dynein light chain-1 and the microtubule-binding domain of the \u03b3 heavy chain shows how axonemal dynein tunes ciliary beating, <em>J. Biol. Chem. <\/em>(2020) <strong>295<\/strong>, 3982-3989<\/li>\n<li>R. Charoenwattanasatien, K. Zinzius, M. Scholz, S. Wicke, H. Tanaka, J.S. Brandenburg, G.M. Marchetti, T. Ikegami, T. Matsumoto, T. Oda, M. Sato, M. Hippler &amp; G. Kurisu, Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga <em>Chlamydomonas reinhardtii. J. Biol. Chem. <\/em>(2020) <strong>295<\/strong>, 170-180<\/li>\n<li>B.S. Hanson, S. Iida, D.J. Read, O.G. Harlen, G. Kurisu, H. Nakamura, S.A. Harris. Continuum mechanical parameterisation of cytoplasmic dynein from atomistic simulation. <em>Methods <\/em>(2020) <strong>185<\/strong>, 39-48<\/li>\n<li>J.M. Schuller, P. Saura, J. Thiemann, S.K. Schuller, A.P. Gamiz-Hernandez, G. Kurisu, M.M. Nowaczyk, V.R.I. Kaila, Redox-coupled proton pumping drives carbon concentration in the photosynthetic complex I. <em>Nature Commun. <\/em>(2020) <strong>11<\/strong>, 494<\/li>\n<li>D. Seo, N. Muraki, G. Kurisu. Kinetic and structural insight into a role of the re-face Tyr328 residue of the homodimeric type ferredoxin-NADP+ oxidoreductase from <em>Rhodopseudomonas palustris <\/em>in the reaction with NADP+\/NADPH <em>Biochim. Biophys. Acta.<\/em> Bioenergetics (2020) <strong>1861<\/strong>, 14140<\/li>\n<li>K. Sugiura, H. Tanaka, G. Kurisu, K.I. Wakabayashi, T. Hisabori. Multicolor redox sensor proteins can visualize redox changes in various compartments of the living cell. <em>Biochim. Biophys. Acta.<\/em> General Subjects (2019) <strong>1863<\/strong>, 1098-1107<\/li>\n<li>M. Brabsztunowicz, P. Mulo, F. Baymann, R. Mutoh, G. Kurisu, P. S\u00e9tif, P. Beyer, A. Krieger-Liszkay. Electron transport pathways in isolated chromoplasts from <em>Narcissus pseudonarcissus<\/em> L. <em>Plant J<\/em>. (2019) <strong>99<\/strong>, 245-256<em><br \/>\n<\/em><\/li>\n<li>J.M. Schuller, J.A. Birrell, H. Tanaka, T. Konuma, H. Wulfhorst, N. Cox, S.K. Schuller, J. Thiemann, W. Lubitz, P. S\u00e9tif, T. Ikegami, B.D. Engel, G. Kurisu &amp; M.M. Nowaczyk Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. <em>Science <\/em>(2019) <strong>363<\/strong>, 257-260<\/li>\n<li>H. Kubota-Kawai, R. Mutoh, K. Shinmura, P. S\u00e9tif, M.M. Nowaczyk, M. R\u00f6gner, T. Ikegami, H. Tanaka, G. Kurisu. X-ray structure of an asymmetric trimeric ferredoxin-photosystem I complex. <em>Nature Plants<\/em> (2018) <strong> 4<\/strong>, 218-224<\/li>\n<li>D.S. Chorev, L.A. Baker, D. Wu, V. Beilsten-Edmands, S.L. Rouse, T. Zeev-Ben-Mordehai, C. Jiko, F. Samsudin, C. Gerle, S. Khalid, A.G. Stewart, S.J. Matthews, K. Gr\u00fcnewald, C.V. Robinson. Protein assemblies ejected directly from native mambranes yield complexes for mass spectrometry. <em>Science<\/em> (2018) <strong> 362<\/strong>, 829-834<\/li>\n<li>R. Quintana-Cabrera, C. Quirin, C. Glytsou, M. Corrado, A. Urbani, A. Pellattiero, E. Calvo, J. V\u00e1zquez, J.A. Enr\u00edquez, C. Gerle, M.E. Soriano, P. Bernardi, L Scorrano. The cristae modulator Optic atrophy 1 requires mitochondrial ATP synthase oligomers to safeguard mitochondrial function.<em> Nature Commun.<\/em>, (2018) <strong>9<\/strong>, 3399<\/li>\n<li>A. Toda, H. Tanaka, G. Kurisu. Structural atlas of dynein motors at atomic resolution. <em>Biophys. Rev<\/em>., (2018) <strong> 2<\/strong>, 677-686<\/li>\n<li>R. Charoenwattanasatien, H. Tanaka, K.Zinzius, A.K. Hochmal, R. Mutoh, D. Yamamoto, M. Hippler, G. Kurisu. X-ray crystallographic and high-speed AFM studies of peroixiredoxin 1 from <em>Chlamydomonas reinhardtii<\/em>. <em>Acta<\/em> <em>Crystallogr.<\/em> Sec. F. (2018) <strong>74<\/strong>, 86-91<\/li>\n<li>L. Mosebach, C. Heilmann, R. Mutoh, P. G\u00e4belein, J. Steinbeck, T. Happe, T. Ikegami, G. Hanke, G. Kurisu and M. Hippler. Association of Ferredoxin:NADP+ oxidoreductase with the photosynthetic apparatus modulates electron transfer in Chlamydomonas reinhardtii. <em>Photosynth. Res<\/em>., (2017) <strong>134<\/strong>, 291-306<\/li>\n<li>P. S\u00e9tif, R. Mutoh, G. Kurisu. Dynamics and energetics of cyanobacterial photosystem I :ferredoxin complexes in different redox states. <em>Biochim. Biophys. Acta Bioenerg<\/em>., (2017) <strong>1858<\/strong>, 483-496<\/li>\n<li>N. Fujieda, T. Nakano, Y. Taniguchi, H. Ichihashi, H. Sugimoto, Y. Morimoto, Y. Nishikawa, G. Kurisu, S. Itoh. A well-defined Osmium-Cupin Complex: Hyperstable Artifical Osmium Peroxygenase.<em> J. Am. Chem. Soc.,<\/em> (2017) <strong>121<\/strong>, 2543-2553<\/li>\n<li>H. Nagashima, H. Kishimoto, R. Mutoh, N. Terashima, H. Oh-Oka, G. Kurisu, H. Mino. Hyperfine Sublevel Correlation Spectroscopy Studies of Iron-Sulfur Cluster in Rieske Protein from Green Sulfur Bacterium <em>Chlorobaculum tepidum<\/em>.<em> J. Phys. Chem. B.<\/em>, (2017) <strong>121<\/strong>, 2543-2553<\/li>\n<li>F. Shinohara, G. Kurisu, G. Hanke, C. Bowsher, T. Hase, Y. Kimata-Ariga. Structural basis for the isotype-specific interactions of ferredoxin and ferredoxin: NADP+ oxidoreductase: an evolutionary switch between photosynthetic and heterotrophic assimilation. <em>Photosynth. Res.<\/em>, (2017) <strong>134<\/strong>, 281-289<\/li>\n<li>M. Kinoshita, J. Y. Kim, S. Kume, Y. Lin, K.H. Mok, Y. Kataoka, K. Ishimori, N. Markova, G. Kurisu, T. Hase, Y.H. Lee. Energetic basis on interactions between ferredoxin and ferredoxin NADP+ reductase at varying physiological conditions. <em>Biochem. Biophys. Res. Commun.<\/em>, (2017) <strong>482<\/strong>, 909-915<\/li>\n<li>J. Y. Kim, M. Kinoshita, S. Kume, H. Gt, T. Sugiki, J.E. Ladbury, C. Kojima, T. Ikegami, G. Kurisu, Y. Goto, T. Hase, Y.H. Lee. Non-covalent forces tune the electron transfer complex between ferredoxin and sulfite reductase to optimize enzymatic activity. <em>Biochem. J.<\/em>, (2016) <strong>473<\/strong>, 3837-3854<\/li>\n<li>C. Mign\u00e9e, R. Mutoh, A. Krieger-Liszkay, G. Kurisu, P. S\u00e9tif. Gallium ferredoxin as a tool to study the effects of ferredoxin binding to photosystem I without ferredoxin reduction. <em>Photosynth. Res.,<\/em> (2017) <strong>134<\/strong>, 251-263<\/li>\n<li>R.A. Ali, A.M. Mehdi, R. Rothnagel, N.A. Hamilton, C. Gerle. M.J. Landsberg, B. Hankamer. RAZA: A Rapid 3D z-crossings algorithm to segment electron tomograms and extract organelles and macromolecules. <em>J. Struct. Biol.<\/em>, (2017) <strong>200<\/strong>, 73-86<\/li>\n<li>N. Kamiya, T. Mashimo, Y. Takano, T. Kon, G. Kurisu, H. Nakamura. Elastic properties of dynein motor domain obtained from all-atom molecular dynamics simulations. <em>Protein Eng. Des. Sel.<\/em>, (2016) <strong>8<\/strong>, 317-325<\/li>\n<li>A. K. Hochmal, K. Zinzius, R. Charoenwattanasatien, P. G\u00e4belein, R. Mutoh, H. Tanaka, S. Schulze, G. Liu, M. Scholz, A. Nordhues, J. N. Offenborn, G. Finazzi, C. Fufezan, K. Huang, G. Kurisu, M. Hippler. Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast. <em>Nature Commun<\/em>., (2016) <strong>7<\/strong>, 11847<\/li>\n<li>R. Charoenwattanasatien, S. Pengthaisong, I. Breen, R. Mutoh, S. Sansenya, Y. Hua, A. Tankrathok, L. Wu, C. Songsirirtthigul, H. Tanaka, S. J. Williams, G. J. Davies, G. Kurisu, J. R. Cairns. Bacterial \u03b2-Glucosidase Reveals the Structural and Functional Basis of Genetic Defects in Human Glucocerebrosidase 2 (GBA2). ACS Chem. Biol., (2016) <strong>11<\/strong>, 1891-1900<\/li>\n<li>J.Y. Kim, M. Nakayama, H. Toyota, G. Kurisu, T. Hase. Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin. <em>J. Biochem.<\/em> (2016) <strong>160<\/strong>, 101-109<\/li>\n<li>Y. Nishikawa, M. Inatomi, H. Iwasaki, G. Kurisu. Structural Change in the Dynein Stalk Region Associated with Two Different Affinities for the Microtubule. <em>J. Mol. Biol.<\/em>, (2016) <strong>428<\/strong>, 1886-1896<\/li>\n<li>J. Esselborn, N. Muraki, K. Klein, V. Engelbrecht, N. Metzler-Nolte, U.-P. Apfel, E. Hofmann, G. Kurisu, T. Happe. A structural view of synthetic cofactor integration into [FeFe]-hydrogenases. <em>Chem. Sci.<\/em>, (2016) <strong>7<\/strong>, 959-968<\/li>\n<li>K. Hirabayashi, E. Yuda, N. Tanaka, S. Katayana, K. Iwasaki, T. Matsumoto, G. Kurisu, F.W. Outten, K. Fukuyama, Y. Takahashi, K. Wada. Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-Binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis. <em>J. Biol. Chem.<\/em>, (2015) <strong>290<\/strong>, 29717-29731<\/li>\n<li>R. Mutoh, N. Muraki, K. Shinmura, H. Kubota-Kawai, Y.H. Lee, M.M. Nowaczyk, M. R\u00f6gner, T. Hase, T. Ikegami, G. Kurisu. X-ray Structure and Nuclear Magnetic Resonance Analysis of the Interaction Sites of the Ga-substituted Cyanobacterial Ferredoxin.<em> Biochemistry<\/em> (2015) <strong>54<\/strong>, 6052-6061<\/li>\n<li>M. Kinoshita, J.Y. Kim, S. Kume, Y. Sakakibara, T. Sugiki, C. Kojima, G. Kurisu, T. Ikegami, T. Hase, Y. Kimata-Ariga, Y.H. Lee. Physicochemical nature of interfaces controlling ferredoxin NADP(+) reductase activity through its interprotein interactions with ferredoxin. <em>Biochim. Biophys. Acta<\/em>. (2015) <strong>1847<\/strong>, 1200-1211<\/li>\n<li>S. Sansenya, R. Mutoh, R. Charoenwattanasatien, G. Kurisu, J. Ketudat-Cairns. Expression and crystallization of a bacterial hydrolase family 116 \u03b2-glucosidase from Thermoanaerobacterium xylanolyticum. <em>Acta Crystallogr.<\/em> Sec. F. (2015) <strong>71<\/strong>, 41-44<\/li>\n<li>S. Uchimura, T. Fujii, H. Takazaki, R. Ayukawa, Y. Nishikawa, I. Minoura, Y. Hachikubo, G. Kurisu, K. Sutoh, T. Kon, K. Namba, E. Muto. A flipped ion pair at the dynein-microtuble interface is critical for dynein motility and ATPase activation. <em>J. Cell. Biol.<\/em> (2015) <strong>208<\/strong>, 211-222<\/li>\n<li>J. E. Siregar, G. Kurisu, T. Kobayashi, M. Matsuzaki, K. Sakamoto, F. Mi-Ichi, Y. I. Watanabe, M. Hirai, H. Matsuoka, D. Syafruddin, S. Marzuki, K. Kita. Direct evidence for the atovaquone action on the Plasmodium cytochrome bc1 complex. <em>Parasitol. Int.<\/em> (2014) in press<\/li>\n<li>Y. Nishikawa, T. Oyama, N. Kamiya, T. Kon, Y.Y. Toyoshima, H. Nakamura and G. Kurisu. Structure of the entire stalk region of the Dynein motor domain. <em>J. Mol. Biol.<\/em>, (2014) <strong>426<\/strong>, 3232-3245<\/li>\n<li>T. Shimegi, T. Oyama, T. Ohtsuki, G. Kurisu, M. Kusunoki and S. Ui. Crystallization and preliminary X-ray diffraction analysis of domain-chimeric L-(2S,3S)-butanediol dehydrogenase. <em>Acta Crystallogr<\/em>. Sect. F. (2014) <strong>70<\/strong>, 461-463<\/li>\n<li>N. Fujieda, S. Yabuta, T. Ikeda, T. Oyama, N. Muraki, G. Kurisu and S. Itoh. Crystal structures of copper-depleted and copper-bound fungal pro-tyrosinase: insights into endogenous cysteine-dependent copper incorporation. <em>J. Biol. Chem.<\/em>, (2013) <strong>288<\/strong>, 22128-22140<\/li>\n<li>Y. Kimata-Ariga, H. Kubota-Kawai, Y. H. Lee, N. Muraki, G. Kurisu and T. Hase. Concentration-dependent oligomerization of cross-linked complexes between ferredoxin and ferredoxin-NADP+ reductase. <em>Biochem., Biophys. Res. Commun<\/em>., (2013) <strong>434<\/strong>, 867-872<\/li>\n<li>R. Narikawa, T. Ishizuka, N. Muraki, T. Shiba, G. Kurisu and M. Ikeuchi. Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism. <em>Proc. Natl. Acad. Sci. USA.<\/em> (2013) <strong>110<\/strong>, 918-923<\/li>\n<li>P. Liauw, T. Mashiba, M. Kopczak, K. Wiegand, N. Muraki, H. Kubota, Y. Kawano, M. Ikeuchi, T. Hase, M. Roegner and G. Kurisu. Cloning, expression, crystallization and preliminary X-ray studies of the ferredoxin-NAD(P)+ reductase from the thermophilic cyanobacterium <em>Thermosynechococcus elongatus<\/em> BP-1. <em>Acta Crystallogr<\/em>. Sect. F. (2012) <strong>68<\/strong>, 1048-1051<\/li>\n<li>M. Twachtmann, B. Altmann, N. Muraki, I. Voss, S. Okutani, G. Kurisu, T. Hase and G. T. Hanke. N-terminal structure of maize ferredoxin:NADP+ reductase determines recruitment into different thylakoid membrane complexes. <em>Plant Cell. <\/em>(2012) <strong>24<\/strong>, 2979-2991<\/li>\n<li>K. Shinmura, N. Muraki, A. Yoshida, T. Hase and G. Kurisu. Crystallization and preliminary X-ray studies of an electron-transfer complex of ferredoxin and ferredoxin-dependent glutamate synthase from the cyanobacterium <em>Leptolyngbya boryana. Acta Crystallogr.<\/em> Sect. F. (2012) <strong>68<\/strong>, 324-327<\/li>\n<li>Y. Sakakibara, H. Kimura, A. Iwamura, T. Saitoh, T. Ikegami, G. Kurisu and T. Hase. A new structural insight into differential interaction of cyanobacterial and plant ferredoxins with nitrite reductase as revealed by NMR and X-ray crystallographic studies. <em>J. Biochem.<\/em>, (2012) <strong>151<\/strong>, 483-492<\/li>\n<li>T. Kon, T. Oyama, R. Shimo-Kon, K. Imamula, T. Shima, K. Sutoh and G. Kurisu. The 2.8 \u00c5 crystal structure of the dynein motor domain. <em>Nature<\/em> (2012) <strong>484<\/strong>, 345-350<\/li>\n<li>W.A. Cramer, S.D. Zakharov, S. Saif Hasan, H. Zhang, D. Baniulis, M.V. Zhalnina, G.M. Soriano, O. Sharma, J.C. Rochet, C. Ryan, J. Whitelegge, G. Kurisu and E. Yamashita. Membrane proteins in four acts: function procedes structure determination. <em>Methods<\/em> (2011) <strong>5<\/strong>, 415-420<\/li>\n<li>T. Kon, K. Sutoh and G. Kurisu. X-ray structure of a functional full-length dynein motor domain., <em>Nature Strut. Mol. Biol.<\/em>, (2011) <strong>18<\/strong>, 638-642<\/li>\n<li>T. Shimegi, Y. Takusagawa, T. Ohtsuki, S. Noda, G. Kurisu, M. Kusunoki and S. Ui., Construction of a tailor-made L(2S,3S)-butanediol dehydrogenase by exchanging domains between native structural analogs. <em>Protein Pept. Lett.<\/em>, (2011) <strong>18<\/strong>, 825-830<\/li>\n<li>M. Okuda, T. Shiba, D.K. Inaoka, K. Kita, G. Kurisu, S. Mineki, S. Harada, S. Watanabe and S. Yoshinari., A conserved lysine residue in the crenarchaea-specific loop is important for the crenarchaeal splicing endonuclease activity.<em> J. Mol. Biol.<\/em>, (2011) <strong>405<\/strong>, 92-104<\/li>\n<li>C. ReinBothe, M. EI Bakkouri, F. Buhr, N. Muraki, J. Nomata, G. Kurisu, Y. Fujita and S. Reinbothe., Chlorophyll biosynthesis: spotlight on protochlorophyllide reduction. <em>Trends Plant Sci<\/em>., (2010) <strong>15,<\/strong> 614-624<\/li>\n<li>N. Muraki, D. Seo, T. Shiba, T. Sakurai and G.Kurisu, Asymmetric Dimeric Structure of Ferredoxin-NAD(P)<sup>+<\/sup> Oxidoreductase from the Green Sulfur Bacterium Chlorobaculum tepidum: Implications for Binding Ferredoxin and NADP<sup>+<\/sup>, <em>J. Mol. Biol.<\/em>, (2010) <strong>401<\/strong>, 403-414<\/li>\n<li>60.N. Muraki, J. Nomata, K. Ebata, T. Mizoguchi, T. Shiba, H. Tamiaki, G. Kurisu and Y. Fujita., X-ray crystal structure of the light-independent protochlorophyllide reductase. <em>Nature<\/em> (2010) advanced online publication<\/li>\n<li>M. Otagiri, S. Ui, Y. Takusagawa, T. Ohtsuki, G. Kurisu and M. Kusunoki. Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases. <em>FEBS Lett.<\/em>, <strong>584<\/strong>, 219-223 (2010)<\/li>\n<li>S. Yoshinari, T. Shiba, D. K. Inaoka, T. Itoh, G. Kurisu, S. Harada, K. Kita and Y. Watanabe, Functional importance of Crenarchaea-specific extra-loop revealed by an X-ray structure of a heterotetrameric crenarchaeal splicing endonuclease, <em>Nucleic Acids Res.<\/em>, <strong>14<\/strong>, 4787-4798 (2009)<\/li>\n<li>R. Narikawa, N. Muraki, T. Shiba, M. Ikeuchi and G. Kurisu, Crystallization and preliminary X-ray studies of the chromophore-binding domain of cyanobacteriochrome AnPixJ from Anabaena sp. PCC 7120, <em>Acta Crystallogr.<\/em> <strong>F65<\/strong>, 159-162 (2009)<\/li>\n<li>D. K. Inaoka, K. Sakamoto, H. Shimizu, T. Shiba, G. Kurisu, T. Nara, T. Aoki, K. Kita and S. Harada, Structures of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction, <em>Biochemistry<\/em> <strong>47<\/strong>, 10881-10891 (2008)<\/li>\n<li>N. Muraki, D. Seo, T. Shiba, T. Sakurai and G. Kurisu, Crystallization and preliminary X-ray studies of ferredoxin-NAD(P)+ reductase from Chlorobium tepidum, <em>Acta Crystallogr. <\/em><strong>F64<\/strong>, 186-189 (2008)<\/li>\n<li>Y. Kimata-Ariga, G. Kurisu, M. Kusunoki, S. Aoki, D. Sato, T. Kobayashi, K. Kita, T. Horii and T. Hase, Cloning and Characterization of Ferredoxin and Ferredoxin-NADP+ Reductase from Human Malaria Parasite, <em>J. Biochem.<\/em>, <strong>141<\/strong>, 421-428 (2007)<\/li>\n<li>W. A. Cramer, H. Zhang, J. Yan, G. Kurisu, E. Yamashita, N. Dashdorj, H. Kim, and S. Savikhin. Structure-Function of the Cytochrome <em>b<\/em>6<em>f<\/em> complex: a design that has worked for three billion years. In Primary Processes of Photosynthesis: Basic Principles and Apparatus (G. Renger, ed.), in Comprehensive Series in Photosciences (D. P. Haeder, series Ed.), pp. 419-448, Royal Society of London, London, UK. 2007.<\/li>\n<li>H. Unno, T. Uchida, H. Sugawara, G. Kurisu, T. Sugiyama, T. Yamaya, H. Sakakibara, T. Hase and M. Kusunoki, Atomic structure of plant glutamine synthetase: a key enzyme for plant productivity. <em>J. Biol. Chem.<\/em>, <strong>281<\/strong>, 29287-29296 (2006)<\/li>\n<li>W. A. Cramer, H. Zhang, J. Yan, G. Kurisu and J. L. Smith, Transmembrane traffic in the cytochrome <em>b<\/em>6<em>f<\/em> complex. <em>Annu. Rev. Biochem.<\/em>,<strong> 75<\/strong>, 769-790 (2006)<\/li>\n<li>J. Yan, G. Kurisu and W. A. Cramer, Intraprotein transfer of the quinine analogue inhibitor 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone in the cytochrome <em>b<\/em>6<em>f<\/em> complex. <em>Proc. Natl. Acad. Sci. U. S. A.<\/em>, <strong>103<\/strong>, 69-74 (2006)<\/li>\n<li>W. A. Cramer, H. Zhang, J. Yan and G. Kurisu, Binding sites of lipophilic quinine and quinine analogue inhibitors in the cytochrome <em>b<\/em>6<em>f<\/em> complex of oxygenic photosynthesis. <em>Biochem., Soc., Trans.<\/em>, <strong>33<\/strong>, 921-923 (2005)<\/li>\n<li>G. Kurisu, , D. Nishiyama, M. Kusunoki, S. Fujikawa, M. Katoh, G. T. Hanke, T. Hase and K. Teshima, A Structural Basis of <em>Equisetum arvense<\/em> Ferredoxin Isoform II Producing an Alternative Electron Transfer with Ferredoxin-NADP+ Reductase. <em>J. Biol. Chem.<\/em>,<strong> 280<\/strong>. 2275-2281 (2005)<\/li>\n<li>W. A. Cramer, J. S. Yan, H. Zhang, G. Kurisu and Smith, J. L. Structure of the cytochrome <em>b<\/em>6<em>f<\/em> complex: new prosthetic groups, Q-space, and the &#8216;hors d&#8217;oeuvres hypothesis&#8217; for assembly of the complex. <em>Photosynthesis Res.<\/em>, <strong>85<\/strong>, 133-144 (2005)<\/li>\n<li>S. Okutani, G. T. Hanke, Y. Satomi, T. Takao, G. Kurisu, A. Suzuki and Hase, T. Three Maize Leaf Ferredoxin:NADPH Oxidoreductases Vary in Subchloroplast Location, Expression, and Interaction with Ferredoxin. <em>Plant Physiol.<\/em>, <strong>139<\/strong>, 1451-1459 (2005)<\/li>\n<li>H. Sugawara, M. Kusunoki, G. Kurisu, T. Fujimoto, H. Aoyagi and T. Hatakeyama. Characteristic recognition of N-acetylgalactosamine by an invertebrate type lection, CEL-I, revealed by X-ray crystallographic analysis. <em>J. Biol. Chem.<\/em>, <strong>279<\/strong>, 45219-45225 (2004)<\/li>\n<li>G. T. Hanke, G. Kurisu, M. Kusunoki and T. Hase. Fd : FNR electron transfer complexes: evolutionary refinement of structural interactions. <em>Photosynthesis Res.<\/em>, <strong>81<\/strong>, 317-327 (2004)<\/li>\n<li>T. Uchida, T. Yamazaki, S. Eto, H. Sugawara, G. Kurisu, A. Nakagawa, M. Kusunoki and T. Hatakeyama. Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate <em>Cucumaria echinata<\/em> : Imprications of domain structure for membrane pore-formation mechanism.<em> J. Biol. Chem.<\/em>, <strong>279<\/strong>, 37133-37141 (2004)<\/li>\n<li>J. L. Smith, H. Zhang, J. S. Yan, G. Kurisu and W. A. Cramer. Cytochrome <em>bc<\/em> complexes: a common core of structure and function surrounded by diversity in the outlying provinces. <em>Current Opin. Struct. Biol.<\/em>, <strong>4<\/strong>, 432-439 (2004)<\/li>\n<li>W. A. Cramer, H. Zhang, J.S. Yan, G. Kurisu and J. L. Smith. Evolution of photosynthesis: Time-independent structure of the cytochrome <em>b<\/em>6<em>f<\/em> complex. <em>Biochemistry<\/em>, <strong>43<\/strong>, 5921-5929 (2004)<\/li>\n<li>G. Kurisu, H. Zhang, J. L. Smith and W. A. Cramer. Structure of the Cytochrome <em>b<\/em>6<em>f<\/em> complex of Oxygenic Photosynthesis: Tuning the cavity.<em> Science,<\/em> <strong>302<\/strong>, 1009-1014 (2003)<\/li>\n<li>G. Kurisu, S. D. Zakharov, M. V. Zhalnina, S. Bano, V. Y. Eroukova, T. I. Rokitskaya, Y. N. Antonenko, M. C. Wiener and W. A. Cramer. The Structure of BtuB with Bound Colicin E3 R-Domain Implies a Translocon. <em>Nature Struct. Biol<\/em>., <strong>10<\/strong>, 948-954 (2003)<\/li>\n<li>K. Teshima, S. Fujita, S. Hirose, D. Nishiyama, G. Kurisu, M. Kusunoki, Y. Kimata-Ariga and T. Hase. A ferredoxin Arg-Glu pair important for efficient electron transfer between ferredoxin and ferredoxin-NADP(+) reductase. <em>FEBS Lett.,<\/em> <strong>546<\/strong>, 189-194 (2003)<\/li>\n<li>H. Miyake, G. Kurisu, M. Kusunoki, S. Nishimura, S. Kitamura, Y. Nitta. Crystal structure of a catalytic site mutant of beta-amylase from <em>Bacillus cereus<\/em> var. mycoides cocrystallized with maltopentaose.<em> Biochemistry<\/em>, <strong>42<\/strong>, 5574-5581 (2003)<\/li>\n<li>H. Zhang, G. Kurisu, J. L. Smith and W. A. Cramer. A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: The cytochrome <em>b<\/em>6<em>f<\/em> complex of oxygenic photosynthesis. <em>Proc. Natl. Acad. Sci. U. S. A.<\/em>, <strong>100<\/strong>, 5160-5163 (2003)<\/li>\n<li>T. Hatakeyama, N. Matsuo, H. Aoyagi, H. Sugawara, T. Uchida, G. Kurisu and M. Kusunoki, Crystallization and preliminary crystallographic study of an invertebrate C-type lectin, CEL-I from the marine invertebrate <em>Cucumaria echinata<\/em>, <em>Acta Crystallogr.<\/em>, <strong>D58<\/strong>, 143-144 (2002)<\/li>\n<li>M. Otagiri, G. Kurisu, S. Swaminathan, S. Ui, S. Yoneda, M. Ohkuma, T. Kudo and M. Kusunoki, Crystallization and preliminary X-ray studies of meso-2,3-butanediol dehydrogenase from <em>Klebsiella pneumoniae <\/em>IAM1063. <em>Acta Crystallogr.<\/em>, <strong>D57<\/strong>, 857-859 (2001)<\/li>\n<li>G. Kurisu, M. Kusunoki, E. Katoh, T. Yamazaki, K. Teshima, Y. Onda, Y. Kimata-Ariga and T. Hase. Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase. <em>Nature Struct. Biol.<\/em>, <strong>8<\/strong>, 117-121 (2001)<\/li>\n<li>M. Otagiri, G. Kurisu, S. Ui, M. Ohkuma, T. Kudo and M. Kusunoki. Crystallization and Preliminary X-ray Studies of L-(+)-2,3-butanediol Dehydrogenase from <em>Brevibacterium saccharolyticum<\/em> C-I012 Protein Peptide Lett., 8, 57-61 (2001)<\/li>\n<li>M. Otagiri, G. Kurisu, S. Ui, Y. Takusagawa, M. Ohkuma, T. Kudo and M. Kusunoki. Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD(+) and inhibitor mercaptoethanol at 1.7 \u00c5 resolution for understanding of chiral substrate recognition mechanisms. <em>J. Biochem<\/em>., <strong>129<\/strong>, 205-208 (2001)<\/li>\n<li>K. Yamamoto, G. Kurisu, M. Kusunoki, S. Tabata, I. Urabe and S. Osaki. Crystal structure of glucose dehydrogenase from <em>Bacillus megaterium<\/em> IWG3 at 1.7 \u00c5 resolution. <em>J. Biochem.,<\/em> <strong>129<\/strong>, 303-312 (2001)<\/li>\n<li>G. Kurisu, Y. Kai and S. Harada. Structure of the zinc-binding site in the crystal structure of a zinc endoprotease from <em>Streptomyces caespitosus<\/em> at 1 \u00c5 resolution. <em>J. Inorg. Biochem.<\/em>, <strong>82<\/strong>, 225-228 (2000)<\/li>\n<li>G. Kurisu, A. Sugimoto, Y. Kai and S. Harada. A flow cell suitable for time-resolved X-ray crystallography by the Laue method. <em>J. Appl. Cryst.<\/em>, <strong>30<\/strong>, 555-556 (1997)<\/li>\n<li>G. Kurisu, A. Sugimoto, S. Harada, M.Takagi, T. Imanaka and Y. Kai. Characterization of a small metalloprotease from <em>Streptomyces caespitosus<\/em> with high specificity to aromatic residues. <em>J. Ferment. Bioeng.<\/em>, <strong>83<\/strong>, 590-592 (1997)<\/li>\n<li>G. Kurisu, T. Kinoshita, A. Sugimoto, A. Nagara, Y. Kai, N. Kasai and S. Harada. Structure of the zinc endoprotease from <em>Streptomyces caespitosus<\/em>. <em>J. Biochem.<\/em>, <strong>121,<\/strong> 304-308 (1997)<\/li>\n<li>S. Harada, A. Nagara, G. Kurisu and Y. Kai. Crystallization and preliminary X-ray studies of a protease from <em>Pseudomonas aeruginosa<\/em>.<em> J. Mol. Biol.<\/em>, <strong>230<\/strong>, 1315-1316 (1993)<\/li>\n<\/ol>\n<\/section>\n","protected":false},"excerpt":{"rendered":"<p>Selected Publication J.M. Schuller, J.A. Birrell, H.Tanaka, T.Konuma, H.Wulfhorst, N.Cox, S.K. Schuller, J. 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