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DOI | 10.2210/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: 17303566DOI: 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) |
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