9HGA

BAM-SurA-darobactin complex in the swing-out state

これはPDB形式変換不可エントリーです。

9HGA の概要

• エントリーDOI: 10.2210/pdb9hga/pdb
• EMDBエントリー: 52132
• 関連するBIRD辞書のPRD_ID: PRD_002330
• 分子名称: Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, ... (7 entities in total)
• 機能のキーワード: insertase, outer membrane protein, chaperone, protein folding, protein complex, darobactin, membrane protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 247636.54

構造登録者

Lehner, P.A.,Jakob, R.P.,Hiller, S. (登録日: 2024-11-19, 公開日: 2025-04-16)

主引用文献

Lehner, P.A.,Degen, M.,Jakob, R.P.,Modaresi, S.M.,Callon, M.,Burmann, B.M.,Maier, T.,Hiller, S.
Architecture and conformational dynamics of the BAM-SurA holo insertase complex.
Sci Adv, 11:eads6094-eads6094, 2025

PubMed Abstract: The proper folding of outer membrane proteins in Gram-negative bacteria relies on their delivery to the β-barrel assembly machinery (BAM) complex. The mechanism by which survival protein A (SurA), the major periplasmic chaperone, facilitates this process is not well understood. We determine the structure of the holo insertase complex, where SurA binds BAM for substrate delivery. High-resolution cryo-electron microscopy structures of four different states and a three-dimensional variability analysis show that the holo insertase complex has a large motional spectrum. SurA bound to BAM can undergo a large swinging motion between two states. This motion is uncoupled from the conformational flexibility of the BamA barrel, which can open and close without affecting SurA binding. Notably, we observed conformational coupling of the SurA swing state and the carboxyl-terminal helix grip domain of BamC. Substrate delivery by SurA to BAM appears to follow a concerted motion that encodes a gated delivery pathway through the BAM accessory proteins to the membrane entry site.

PubMed: 40184469
DOI: 10.1126/sciadv.ads6094

実験手法

ELECTRON MICROSCOPY (3.62 Å)