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Behavior of water molecules in ATPase pocket of myosin 

作成者 Yamanaka, Kazunori, Okimoto, Noriaki, Hata, Masayuki, Neya, Saburo, Hoshino, Tyuji
作成者の別表記 畑, 昌之, 根矢, 三郎, 星野, 忠次
キーワード等 water molecules, molecular dynamics, hydrolysis, salt bridge, myosin
日本十進分類法 (NDC) 490
内容 Not a single water molecule but a group of water molecules frequently play an importantrole to functionalize the enzymatic reaction of proteins. In this study, we carried out molecular dynamics(MD) simulations for 4 types of myosin-nucleotide complexes; the ATP and/or ADP/Pi-bound myosins withthe cleft open and/or close conformations. Computational results show a keen role of water moleculesthose are regulated by a salt-bridge formed between Arg238 in Switch I and Glu459 in Switch II. Before theATP hydrolysis, Arg238 and Glu459 hold a lytic water near ATP-g phosphate and close the salt-bridge toinhibit any other water to enter the ATPase pocket except one water that controls the orientation of the lyticwater facing to ATP. Once the salt-bridge is opened after ATP hydrolysis, a large number of watermolecules are circulating in the ATPase pocket. Our results demonstrate that the access of watermolecules is precisely controlled in the respective reaction step of the ATP hydrolysis cycle.
作成日付 2006
コンテンツの種類 雑誌掲載論文 Journal Article
DCMI資源タイプ text
ファイル形式 application/pdf
ハンドルURL http://mitizane.ll.chiba-u.jp/meta-bin/mt-pdetail.cgi?cd=00023224
ISSN 0166-1280
掲載誌情報 Journal of Molecular Structure: THEOCHEM Vol.758 page.97-105 (2006)
フルテキストへのリンク http://mitizane.ll.chiba-u.jp/metadb/up/hoshino/Manuscript2005Sep30.pdf
言語 英語
著者版フラグ author


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water molecules
molecular dynamics
hydrolysis
salt bridge
myosin