6E52

Chimeric structure of Saccharomyces cerevisiae GCN4 leucine zipper fused to Staphylococcus aureus AgrC cytoplasmic histidine kinase module (dataset anisotropically truncated by STARANISO)

6E52 の概要

• エントリーDOI: 10.2210/pdb6e52/pdb
• 分子名称: Staphylococcus aureus AgrC histidine kinase module fused to Saccharomyces cerevisiae GCN4 leucine zipper (2 entities in total)
• 機能のキーワード: protein histidine kinase, bacterial quorum sensing, coiled coil, bergerat fold, signaling protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57687.74

構造登録者

Xie, Q.,Jeffrey, P.D.,Muir, T.W. (登録日: 2018-07-19, 公開日: 2019-02-27, 最終更新日: 2024-03-13)

主引用文献

Xie, Q.,Zhao, A.,Jeffrey, P.D.,Kim, M.K.,Bassler, B.L.,Stone, H.A.,Novick, R.P.,Muir, T.W.
Identification of a Molecular Latch that Regulates Staphylococcal Virulence.
Cell Chem Biol, 26:548-558.e4, 2019

PubMed Abstract: Virulence induction in the Staphylococcus aureus is under the control of a quorum sensing (QS) circuit encoded by the accessory gene regulator (agr) locus. Allelic variation within agr produces four QS specificity groups, each producing a unique secreted autoinducer peptide (AIP) and receptor histidine kinase (RHK), AgrC. Cognate AIP-AgrC interactions activate virulence through a two-component signaling cascade, whereas non-cognate pairs are generally inhibitory. Here we pinpoint a key hydrogen-bonding interaction within AgrC that acts as a switch to convert helical motions propagating from the receptor sensor domain into changes in inter-domain association within the kinase module. AgrC mutants lacking this interaction are constitutively active in vitro and in vivo, the latter leading to a pronounced attenuation of S. aureus biofilm formation. Thus, our work sheds light on the regulation of this biomedically important RHK.

PubMed: 30773482
DOI: 10.1016/j.chembiol.2019.01.006

実験手法

X-RAY DIFFRACTION (1.93 Å)