2011 Fiscal Year Final Research Report
Structural and functional basis of the complex of mono-ADP-ribosylating toxin and substrate protein
Project/Area Number |
21570121
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Kyoto Sangyo University (2010-2011) Tokushima Bunri University (2009) |
Principal Investigator |
TSUGE Hideaki 京都産業大学, 総合生命科学部, 教授 (40299342)
|
Co-Investigator(Renkei-kenkyūsha) |
SAKURAI Jun 徳島文理大学, 薬学部, 教授 (80029800)
NAGAHAMA Masahiro 徳島文理大学, 薬学部, 教授 (40164462)
ODA Masataka 徳島文理大学, 薬学部, 講師 (00412403)
|
Research Collaborator |
TSURUMURA Toshiharu 京都産業大学, 総合生命科学部, プロジェクト助教 (50450250)
|
Project Period (FY) |
2009 – 2011
|
Keywords | C3 / RhoA / Ia / アクチン / モノADPリボシル化 / 結晶構造解析 / 特異性 |
Research Abstract |
To reveal the structural and functional mechanism of C. perfringens iota toxin(Ia) and actin, we successfully crystallized and solved the structure of the apo-Ia-actin and apo-Ia. We revealed the structural change upon the ADP-ribosylation by comparing the structures together with NADH-Ia and βTAD-Ia-actin complex. C. Botulinum C3 toxin ADP-ribosylates RhoA Asn41. For the structure analysis of C3-RhoA complex, RhoA was expressed in E. coli and the stable mutant of RhoAF25N was obtained using His-tag and GST-tag, independently. We are currently searching the crystallization condition for the complex.
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Research Products
(23 results)