Osaka University Institute for Protein Research
Tsukihara Lab

Welcome to Tsukihara Lab!

The aim of this laboratory is to elucidate the protein structure-function relationships and to establish general principles for protein architecture.
Professors, researchers and graduate students here cooperate and work together to explore mystery of life.

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Research Subjects

Three-dimensional protein structure brings us the beautiful structural biology. X-ray crystallography is the best method to determine atomic coordinates of protein molecules. The main aim of our reserch is the X-ray structure determination of the biological macromolecular assemblies including membrane protein complexes, in order to elucidate the molecular mechanism of the highly organized biological processes at atomic level.

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In 1995 Dr.Tsukihara succeeded in structural determination of Bovine heart cytochrome c oxidase, which was the first mammalian membrane protein structure determined.

Reserach Activities

: : C:\Users\tsutsui\Desktop\parts\bullet035.gifCrystal Structure Analysis of Bovine Cytochrome c Oxidase
Bovine cytochrome c oxidase is a large multicomponent membrane protein complex functioning as a dimer with a molecular weight of 400K daltons comprising two copies of 13 different subunits. We have determined crystal structures of several states of the enzyme. Higher resolution analyses are in progress to elucidate the molecular mechanism of respiration.

: : C:\Users\tsutsui\Desktop\parts\bullet035.gifCrystal Structure Analysis of Bovine Proteasome
Eukaryotic 20S proteasomes are multicatalitic proteinase complex with a molecular weight of 750K daltons, containing respectively, two copies of a hetero-heptamer of -type subunits and that of -type subunits,(1-7 1-7).We have determined the crystal structure of the enzyme purified from bovine liver. The enzyme exists in the cell as 26S proteasome with a molecular weight of 2300KDa. Crystallization of 26S proteasome is in progress.

: : C:\Users\tsutsui\Desktop\parts\bullet035.gifCrystal Structure Analysis of Rice Dwarf Virus
Rice dwarf virus(RDV)is a double-shelled spherical plant virus with a molecular weight of 75,000K daltons. We have determined the novel structure of the virus at 3.5
resolution.
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: : C:\Users\tsutsui\Desktop\parts\bullet035.gifStudies on the Structure-Function Relationships of a-Amylase and Related Enzymes
We have so far determined the structures of a-Amylases and related enzymes; Taka-amylase, B. thermophillus cyclodextrin glucanotransferase, P.stutzeri maltotetraose-forming a-amylase, and recently Pseudomonas isoamylase. Through these structure analyses, the specificitiese of their substrate binding and the catalytic mechanism have been clarified using mutant enzymes when necessary. We are extending there structural studies for other important mutants and also for other kind of a-amylase family enzymes in collaboration with biochemists.


Results of Research
(Papers)

Professor Tomitake Tsukihara's Profile

Laboratory Members

Seminars & Events

Admission

Links

Access to the Institute

Tsukihara@Lab
Institute for Protein Research, Osaka University


Address: 3-2 Yamadaoka, Suita, Osaka 565-0871, JAPAN
Phone: +81-6-6879-4331 Fax: +81-6-6879-4331
E-mail: tsuki*protein.osaka-u.ac.jp
(Please replace * by @)

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