8BWC

E. coli BAM complex (BamABCDE) wild-type

8BWC の概要

• エントリーDOI: 10.2210/pdb8bwc/pdb
• EMDBエントリー: 16282
• 分子名称: Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, ... (5 entities in total)
• 機能のキーワード: outer membrane protein, protein folding, beta barrel, membrane protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 200226.02

構造登録者

Machin, J.M.,Radford, S.E.,Ranson, N.A. (登録日: 2022-12-06, 公開日: 2023-05-24, 最終更新日: 2023-09-06)

主引用文献

Haysom, S.F.,Machin, J.,Whitehouse, J.M.,Horne, J.E.,Fenn, K.,Ma, Y.,El Mkami, H.,Bohringer, N.,Schaberle, T.F.,Ranson, N.A.,Radford, S.E.,Pliotas, C.
Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells.
Angew.Chem.Int.Ed.Engl., 62:e202218783-e202218783, 2023

PubMed Abstract: The β-barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram-negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane (OM). Here, we use Pulsed Electron-Electron Double Resonance (PELDOR, or DEER) spectroscopy distance measurements to interrogate the conformational ensemble of the BAM complex in E. coli cells. We show that BAM adopts a broad ensemble of conformations in the OM, while in the presence of the antibiotic darobactin B (DAR-B), BAM's conformational equilibrium shifts to a restricted ensemble consistent with the lateral closed state. Our in-cell PELDOR findings are supported by new cryoEM structures of BAM in the presence and absence of DAR-B. This work demonstrates the utility of PELDOR to map conformational changes in BAM within its native cellular environment.

PubMed: 37162386
DOI: 10.1002/anie.202218783

実験手法

ELECTRON MICROSCOPY (3.5 Å)