4UEY

Structure of the periplasmic domain PhoQ double mutant (W104C-A128C)

4UEY の概要

• エントリーDOI: 10.2210/pdb4uey/pdb
• 分子名称: PHOQ PERIPLASMIC DOMAIN DOUBLE MUTANT (2 entities in total)
• 機能のキーワード: signaling protein, signal transduction, phoq, periplasmic domain, hamp domain, histidine kinase
• 由来する生物種: SALMONELLA ENTERICA
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : P0DM80
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 53514.60

構造登録者

Sancho-Vaello, E.,Hicks, K.G.,Miller, S.I.,Zeth, K. (登録日: 2014-12-21, 公開日: 2015-06-24, 最終更新日: 2024-11-06)

主引用文献

Hicks, K.G.,Delbecq, S.P.,Sancho-Vaello, E.,Blanc, M.P.,Dove, K.K.,Prost, L.R.,Daley, M.E.,Zeth, K.,Klevit, R.E.,Miller, S.I.
Acidic pH and divalent cation sensing by PhoQ are dispensable for systemic salmonellae virulence.
Elife, 4:e06792-e06792, 2015

PubMed Abstract: Salmonella PhoQ is a histidine kinase with a periplasmic sensor domain (PD) that promotes virulence by detecting the macrophage phagosome. PhoQ activity is repressed by divalent cations and induced in environments of acidic pH, limited divalent cations, and cationic antimicrobial peptides (CAMP). Previously, it was unclear which signals are sensed by salmonellae to promote PhoQ-mediated virulence. We defined conformational changes produced in the PhoQ PD on exposure to acidic pH that indicate structural flexibility is induced in α-helices 4 and 5, suggesting this region contributes to pH sensing. Therefore, we engineered a disulfide bond between W104C and A128C in the PhoQ PD that restrains conformational flexibility in α-helices 4 and 5. PhoQ(W104C-A128C) is responsive to CAMP, but is inhibited for activation by acidic pH and divalent cation limitation. phoQ(W104C-A128C) Salmonella enterica Typhimurium is virulent in mice, indicating that acidic pH and divalent cation sensing by PhoQ are dispensable for virulence.

PubMed: 26002083
DOI: 10.7554/eLife.06792

実験手法

X-RAY DIFFRACTION (1.9 Å)