『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
ID: Pass:

登録内容 (EID=154905)

EID=154905EID:154905, Map:0, LastModified:2012年9月4日(火) 14:47:20, Operator:[大家 隆弘], Avail:TRUE, Censor:0, Owner:[木戸 博], Read:継承, Write:継承, Delete:継承.
種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
招待 (推奨):
審査 (推奨):
カテゴリ (推奨):
共著種別 (推奨):
学究種別 (推奨):
組織 (推奨): 1.徳島大学.分子酵素学研究センター (〜2007年3月31日/->組織[徳島大学.疾患酵素学研究センター]) [継承]
著者 (必須): 1. (英) Wu Xueji (日) (読)
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
2.矢野 仁康
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
3. (英) Washida H. (日) (読)
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
4.木戸 博 ([徳島大学.先端酵素学研究所.重点研究部門])
役割 (任意):
貢献度 (任意):
学籍番号 (推奨):
[継承]
題名 (必須): (英) The second metal-binding site of 70kDa heat-shock protein is essential for ADP-binding, ATP hydrolysis and ATP synthesis  (日)    [継承]
副題 (任意):
要約 (任意): (英) The chaperone activity of Hsp70 (70 kDa heat-shock protein) in protein folding and its conformational switch, including oligomeric and monomeric interconversion, are regulated by the hydrolysis of ATP and the ATP-ADP exchange cycle. The crystal structure of human ATPase domain shows two metal-binding sites, the first for ATP binding and a second, in close proximity to the first, whose function remains unknown [Sriram, Osipiuk, Freeman, Morimoto and Joachimiak (1997) Structure 5, 403-414]. In this study, we have characterized the second metal-binding motif by site-directed mutagenesis and the kinetics of ATP and ADP binding, and found that the second metal-binding site, comprising a loop co-ordinated by His-227, Glu-231 and Asp-232, participates both in ATP hydrolysis and ATP-synthetic activities, in co-operation with the first metal-binding site. The first metal-binding site, a catalytic centre, is essential for ATP binding and the second site for ADP binding in the reactions of ATP hydrolysis and ATP synthesis.  (日)    [継承]
キーワード (推奨): 1. (英) Adenosine Diphosphate (日) (読) [継承]
2. (英) Adenosine Triphosphate (日) (読) [継承]
3. (英) Binding Sites (日) (読) [継承]
4. (英) Escherichia coli (日) (読) [継承]
5. (英) HSP70 Heat-Shock Proteins (日) (読) [継承]
6. (英) Humans (日) (読) [継承]
7. (英) Hydrolysis (日) (読) [継承]
8. (英) Metals (日) (読) [継承]
9. (英) Mutagenesis, Site-Directed (日) (読) [継承]
10. (英) Nucleoside-Diphosphate Kinase (日) (読) [継承]
11. (英) Recombinant Proteins (日) (読) [継承]
12. (英) Temperature (日) (読) [継承]
発行所 (推奨):
誌名 (必須): The Biochemical Journal ([The Biochemical Society])
(pISSN: 0264-6021, eISSN: 1470-8728)

ISSN (任意): 1470-8728
ISSN: 0264-6021 (pISSN: 0264-6021, eISSN: 1470-8728)
Title: The Biochemical journal
Title(ISO): Biochem J
Publisher: Portland Press, Ltd.
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
[継承]
[継承]
(必須): 378 [継承]
(必須): Pt 3 [継承]
(必須): 793 799 [継承]
都市 (任意):
年月日 (必須): 西暦 2004年 4月 1日 (平成 16年 4月 1日) [継承]
URL (任意):
DOI (任意): 10.1042/BJ20031680    (→Scopusで検索) [継承]
PMID (任意): 14664695    (→Scopusで検索) [継承]
NAID (任意):
WOS (任意):
Scopus (任意):
評価値 (任意):
被引用数 (任意):
指導教員 (推奨):
備考 (任意): 1.(英) Article.Affiliation: Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima 770-8503, Japan.  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]
4.(英) OtherID: PMC1224023  (日)    [継承]

標準的な表示

和文冊子 ● Xueji Wu, Mihiro Yano, H. Washida and Hiroshi Kido : The second metal-binding site of 70kDa heat-shock protein is essential for ADP-binding, ATP hydrolysis and ATP synthesis, The Biochemical Journal, Vol.378, No.Pt 3, 793-799, 2004.
欧文冊子 ● Xueji Wu, Mihiro Yano, H. Washida and Hiroshi Kido : The second metal-binding site of 70kDa heat-shock protein is essential for ADP-binding, ATP hydrolysis and ATP synthesis, The Biochemical Journal, Vol.378, No.Pt 3, 793-799, 2004.

関連情報

Number of session users = 6, LA = 2.04, Max(EID) = 382152, Max(EOID) = 1020840.