Laboratory of Protein Crystallography

Member

Director Genji KURISU
Associate Professor Hideaki TANAKA
Christoph GERLE
Technical Staff  Naoko NORIOKA

 

Correspondence

Tel 81-6-6879-8604
Fax 81-6-6879-8606
E-mail
URL http://www.protein.osaka-u.ac.jp/crystallography/EngHP/

Research

In the 1959 the division of Protein Crystallography was established to elucidate the molecular structure of proteins by X-ray crystal structure analysis. The X-ray method has become the most powerful tool to determine protein structure. One of our aims is to spread the application of this method throughout biological science. Our own research targets are focused on biological macromolecular assemblies and membrane proteins. All of these are long term and important projects.

06_1
Fig. 1: Crystal structure of the hetero-tetrameric catalytic component NB-protein of DPOR (Dark-operative Protochlorophyllide OxidoReductase). The [4Fe-4S] clusters are shown in CPK model, and the Pchlide molecules in stick model. The BchN and BchB subunits in one dimer are colored in green and blue (Nature 456, 110-114, 2010).
kurisulabHP1dynein0091
Fig. 2: Overall structure of the cytoplasmic dynein motor domain depicted with the model of a microtubule.The force-generating rod-like linker, the ATP-hydrolyzing ring and the dynein specific C-sequence units are located sequentially from the N-terminus. Characteristic Y-shaped structure called “stalk and strut coiled-coils” are inserted into the AAA4 and AAA5 modules (Nature 484, 345-350, 2012).

Current Research Programs

  1. Structural studies of photosynthetic energy-transducing membrane and related redox enzymes
  2. Crystal structure analyses of dynein motors
  3. High resolution structural analysis of rat liver vault

References

  1. The Structure of Rat Liver Vault at 3.5 Angstrom Resolution. Tanaka, H. et al., (2009) Science 323, 384-388
  2. X-ray crystal structure of the light-independent protochlorophyllide reductase. Muraki, N. et al., (2010) Nature 465, 110-114
  3. The 2.8 Å crystal structure of the dynein motor domain. Kon, T. et al., (2012) Nature 484, 345-350