5EKQ

The structure of the BamACDE subcomplex from E. coli

5EKQ の概要

• エントリーDOI: 10.2210/pdb5ekq/pdb
• 分子名称: Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamD, Outer membrane protein assembly factor BamC, ... (4 entities in total)
• 機能のキーワード: membrane protein, insertase, beta-barrel, outer membrane protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 159124.36

構造登録者

Bakelar, J.,Buchanan, S.K.,Noinaj, N. (登録日: 2015-11-04, 公開日: 2016-01-20, 最終更新日: 2024-10-30)

主引用文献

Bakelar, J.,Buchanan, S.K.,Noinaj, N.
The structure of the beta-barrel assembly machinery complex.
Science, 351:180-186, 2016

PubMed Abstract: β-Barrel outer membrane proteins (OMPs) are found in the outer membranes of Gram-negative bacteria and are essential for nutrient import, signaling, and adhesion. A 200-kilodalton five-component complex called the β-barrel assembly machinery (BAM) complex has been implicated in the biogenesis of OMPs. We report the structure of the BAM complex from Escherichia coli, revealing that binding of BamCDE modulates the conformation of BamA, the central component, which may serve to regulate the BAM complex. The periplasmic domain of BamA was in a closed state that prevents access to the barrel lumen, which indicates substrate OMPs may not be threaded through the barrel during biogenesis. Further, conformational shifts in the barrel domain lead to opening of the exit pore and rearrangement at the lateral gate.

PubMed: 26744406
DOI: 10.1126/science.aad3460

実験手法

X-RAY DIFFRACTION (3.392 Å)