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2J70

Structural and functional characterisation of partner-switching regulating the environmental stress response in B. subtilis

2J70 の概要
エントリーDOI10.2210/pdb2j70/pdb
関連するPDBエントリー1W53 2J6Y 2J6Z
分子名称PHOSPHOSERINE PHOSPHATASE RSBU (2 entities in total)
機能のキーワードenvironmental stress response, partner switching, protein phosphatase, rsbt, rsbu, hydrolase, bacillus subtilis
由来する生物種BACILLUS SUBTILIS
タンパク質・核酸の鎖数1
化学式量合計13193.04
構造登録者
Hardwick, S.W.,Pane-Farre, J.,Delumeau, O.,Marles-Wright, J.,Murray, J.W.,Hecker, M.,Lewis, R.J. (登録日: 2006-10-05, 公開日: 2007-02-13, 最終更新日: 2023-12-13)
主引用文献Hardwick, S.W.,Pane-Farre, J.,Delumeau, O.,Marles-Wright, J.,Murray, J.W.,Hecker, M.,Lewis, R.J.
Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.
J. Biol. Chem., 282:11562-11572, 2007
Cited by
PubMed Abstract: The general stress response of Bacillus subtilis and close relatives provides the cell with protection from a variety of stresses. The upstream component of the environmental stress signal transduction cascade is activated by the RsbT kinase that switches binding partners from a 25 S macromolecular complex, the stressosome, to the RsbU phosphatase. Once the RsbU phosphatase is activated by interacting with RsbT, the alternative sigma factor, sigmaB, directs transcription of the general stress regulon. Previously, we demonstrated that the N-terminal domain of RsbU mediates the binding of RsbT. We now describe residues in N-RsbU that are crucial to this interaction by experimentation both in vitro and in vivo. Furthermore, crystal structures of the N-RsbU mutants provide a molecular explanation for the loss of interaction. Finally, we also characterize mutants in RsbT that affect binding to both RsbU and a simplified, binary model of the stressosome and thus identify overlapping binding surfaces on the RsbT "switch."
PubMed: 17303566
DOI: 10.1074/jbc.M609733200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.95 Å)
構造検証レポート
Validation report summary of 2j70
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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