9MGF

beta-barrel assembly machine from Escherichia coli in a middle state of substrate assembly

9MGF の概要

• エントリーDOI: 10.2210/pdb9mgf/pdb
• EMDBエントリー: 48254
• 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: beta-barrel assembly machine, outer membrane, folding intermediate, 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: 263758.77

構造登録者

Thomson, B.D.,Kahne, D. (登録日: 2024-12-10, 公開日: 2025-12-17, 最終更新日: 2025-12-24)

主引用文献

Thomson, B.D.,Marquez, M.D.,Rawson, S.,Dos Santos, T.M.A.,Harrison, S.C.,Kahne, D.
Structures of folding intermediates on BAM show diverse substrates fold by a uniform mechanism.
Biorxiv, 2025

PubMed Abstract: The outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria contain β-barrel membrane proteins that are assembled by conserved multi-subunit machines. In bacteria, the β-barrel assembly machine (BAM) folds over a hundred compositionally different substrates into barrels that vary greatly in size. Some larger barrels require globular proteins to plug the barrel lumen. How a single machine can assemble such different barrels is unknown. Here we report three structures representing progressively folded stages of a 16-stranded barrel engaged with BAM, as well as the structure of a late-stage folding intermediate of a 26-stranded substrate folding around its soluble lipoprotein plug on BAM. We find that BAM catalyzes folding of these substrates by a uniform mechanism in which BAM undergoes major distortions to accommodate the nascent barrel.

PubMed: 41280068
DOI: 10.1101/2025.10.16.682720

実験手法

ELECTRON MICROSCOPY (3.3 Å)