| 1.Research Institution | Kyoto University | |
| 2.Research Area | Life Sciences | |
| 3.Research Field | Structure and Functional Control Mechanism of Biomolecules (Structural Biology and Functional Molecules) | |
| 4.Term of Project | FY 1997 〜 FY 2001 | |
| 5.Project Number | 97L00501 | |
| 6.Title of Project | X-ray Crystallographic Study on Biological Molecular Interaction |
| Name | Institution,Department | Title of Position |
| Kunio Miki | Kyoto University, Graduate School of Science | Professor |
8.Core Members
| Names | Institution,Department | Title of Position |
| Isao Tanaka | Hokkaido University, Graduate School of Science | Professor |
| Akira Yasui | Tohoku University, Institute of Development, Aging and Cancer | Professor |
| Tooru Taga | Kyoto University, Graduate School of Pharmaceutical Sciences | Professor |
9.Summary of Research Results
|
The aim of the project is to understand a variety of biological molecular interactions on the basis
of the three-dimensional structures of protein molecules determined by X-ray crystallography.
Biological molecular interactions include protein and protein, protein and nucleic acid and
protein and small molecule (substrate, metal, cofactors etc.) interactions. We have determined
the three-dimensional structures of the following proteins and protein complexes and discussed
their structure-function relationship; chaperonin-60, thermosome α subunit complex,
thermophilic photosynthetic reaction center and high potential iron-sulfur protein, and
lipoprotein localization factors, LolA and LolB for protein and protein interactions, cyanobacterial
DNA photolyase, and photolyase from a thermophilic bacterium and its complex with thymine,
and a complex between DNA replication initiation protein RepE and DNA for protein and DNA
interactions, and metapyrocatechase (a dioxygenase), human secretory phospholipase A2-IIA
complex with a potent indolizine inhibitor, chitosanase, undecaprenyl diphosphate synthase,
ribulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon (Rubisco),
aldehyde reductase from a red yeast, a complex between calyculin A and the catalytic subunit of
protein phosphatase 1, novel alkaline serine protease and α-amylase, and S100 family proteins,
NRP8 and MRP14 for protein and small molecule interactions. We have extensively discussed
about the reaction mechanism and molecular recognition controlled by the above protein
molecules. In addition, it was found that mammalian photolyase homologues are essential for
maintenance of circadian rhythms and their structural studies are now in progress.
Synchrotron radiation, especially that in SPring-8 has been extensively used in this project, in
which several effective techniques were developed. |
10.Key Words
(1)X-ray crystallography、(2)three-dimensional structure、(3)synchrotron radiation facility
(4)protein-protein interaction、(5)protein-DNA interaction、(6)enzyme-substrate interaction
(7)DNA photolyase、(8)DNA replication initiator、(9)S100 family