9AVI

TolQ inner membrane protein from Acinetobacter baumannii

9AVI の概要

• エントリーDOI: 10.2210/pdb9avi/pdb
• EMDBエントリー: 43902
• 分子名称: Tol-Pal system protein TolQ (1 entity in total)
• 機能のキーワード: inner membrane protein complex, structural genomics, center for structural biology of infectious diseases, csbid, membrane protein
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 126950.96

構造登録者

Quade, B.,Otwinowski, Z.,Borek, D.,Center for Structural Biology of Infectious Diseases (CSBID) (登録日: 2024-03-03, 公開日: 2025-01-22, 最終更新日: 2025-04-16)

主引用文献

Karimullina, E.,Guo, Y.,Khan, H.M.,Emde, T.,Quade, B.,Di Leo, R.,Otwinowski, Z.,Tieleman, D.P.,Borek, D.,Savchenko, A.
Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogen Acinetobacter baumannii.
Sci Adv, 11:eadq9845-eadq9845, 2025

PubMed Abstract: Gram-negative bacteria harness the proton motive force (PMF) within their inner membrane (IM) to uphold cell envelope integrity, an indispensable aspect for both division and survival. The IM TolQ-TolR complex is the essential part of the Tol-Pal system, serving as a conduit for PMF energy transfer to the outer membrane. Here we present cryo-electron microscopy reconstructions of TolQ in apo and TolR-bound forms at atomic resolution. The apo TolQ configuration manifests as a symmetric pentameric pore, featuring a transmembrane funnel leading toward a cytoplasmic chamber. In contrast, the TolQ-TolR complex assumes a proton nonpermeable stance, characterized by the TolQ pentamer's flexure to accommodate the TolR dimer, where two protomers undergo a translation-based relationship. Our structure-guided analysis and simulations support the rotor-stator mechanism of action, wherein the rotation of the TolQ pentamer harmonizes with the TolR protomers' interplay. These findings broaden our mechanistic comprehension of molecular stator units empowering critical functions within the Gram-negative bacterial cell envelope.

PubMed: 40184442
DOI: 10.1126/sciadv.adq9845

実験手法

ELECTRON MICROSCOPY (3.02 Å)