4IF4

Crystal Structure of the Magnesium and beryllofluoride-activated VraR from Staphylococcus aureus

4IF4 の概要

• エントリーDOI: 10.2210/pdb4if4/pdb
• 関連するPDBエントリー: 4GVP
• 分子名称: Response regulator protein VraR, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION, ... (5 entities in total)
• 機能のキーワード: response regulator, two-component system, bacterial signalling, dna binding, transcription factor, transcription regulation, phosphorylation, transcription
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Cytoplasm (Potential): Q7A2Q1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 94586.08

構造登録者

Leonard, P.G.,Stock, A.M. (登録日: 2012-12-14, 公開日: 2013-05-08, 最終更新日: 2024-02-28)

主引用文献

Leonard, P.G.,Golemi-Kotra, D.,Stock, A.M.
Phosphorylation-dependent conformational changes and domain rearrangements in Staphylococcus aureus VraR activation.
Proc.Natl.Acad.Sci.USA, 110:8525-8530, 2013

PubMed Abstract: Staphylococcus aureus VraR, a vancomycin-resistance-associated response regulator, activates a cell-wall-stress stimulon in response to antibiotics that inhibit cell wall formation. X-ray crystal structures of VraR in both unphosphorylated and beryllofluoride-activated states have been determined, revealing a mechanism of phosphorylation-induced dimerization that features a deep hydrophobic pocket at the center of the receiver domain interface. Unphosphorylated VraR exists in a closed conformation that inhibits dimer formation. Phosphorylation at the active site promotes conformational changes that are propagated throughout the receiver domain, promoting the opening of a hydrophobic pocket that is essential for homodimer formation and enhanced DNA-binding activity. This prominent feature in the VraR dimer can potentially be exploited for the development of novel therapeutics to counteract antibiotic resistance in this important pathogen.

PubMed: 23650349
DOI: 10.1073/pnas.1302819110

実験手法

X-RAY DIFFRACTION (2.35 Å)