3HSR

Crystal structure of Staphylococcus aureus protein SarZ in mixed disulfide form

3HSR の概要

• エントリーDOI: 10.2210/pdb3hsr/pdb
• 関連するPDBエントリー: 3HRM 3HSE
• 分子名称: HTH-type transcriptional regulator sarZ, benzenethiol, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: helix-turn-helix, cysteine disulfide, marr-family transcriptional regulator, dna-binding, transcription, transcription regulation, transcription regulator
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66670.81

構造登録者

Poor, C.B.,Duguid, E.,Rice, P.A.,He, C. (登録日: 2009-06-10, 公開日: 2009-07-07, 最終更新日: 2024-11-06)

主引用文献

Poor, C.B.,Chen, P.R.,Duguid, E.,Rice, P.A.,He, C.
Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus.
J.Biol.Chem., 284:23517-23524, 2009

PubMed Abstract: SarZ is a global transcriptional regulator that uses a single cysteine residue, Cys(13), to sense peroxide stress and control metabolic switching and virulence in Staphylococcus aureus. SarZ belongs to the single-cysteine class of OhrR-MgrA proteins that play key roles in oxidative resistance and virulence regulation in various bacteria. We present the crystal structures of the reduced form, sulfenic acid form, and mixed disulfide form of SarZ. Both the sulfenic acid and mixed disulfide forms are structurally characterized for the first time for this class of proteins. The Cys(13) sulfenic acid modification is stabilized through two hydrogen bonds with surrounding residues, and the overall DNA-binding conformation is retained. A further reaction of the Cys(13) sulfenic acid with an external thiol leads to formation of a mixed disulfide bond, which results in an allosteric change in the DNA-binding domains, disrupting DNA binding. Thus, the crystal structures of SarZ in three different states provide molecular level pictures delineating the mechanism by which this class of redox active regulators undergoes activation. These structures help to understand redox-mediated virulence regulation in S. aureus and activation of the MarR family proteins in general.

PubMed: 19586910
DOI: 10.1074/jbc.M109.015826

実験手法

X-RAY DIFFRACTION (1.9 Å)