5LJO

E. coli BAM complex (BamABCDE) by cryoEM

5LJO の概要

• エントリーDOI: 10.2210/pdb5ljo/pdb
• EMDBエントリー: 4061
• 分子名称: Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, Outer membrane protein assembly factor BamD, ... (5 entities in total)
• 機能のキーワード: membrane protein, bam, omp, beta barrel, outer membrane, gram negative
• 由来する生物種: Escherichia coli K12; 詳細
• 細胞内の位置: Cell outer membrane ; Lipid-anchor : P77774 P0A903 P0AC04 P0A938; Cell outer membrane : B7MBF8
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 180072.79

構造登録者

Iadanza, M.G.,Ranson, N.A.,Radford, S.E.,Higgins, A.J.,Schffrin, B.,Calabrese, A.N.,Ashcroft, A.E.,Brockwell, D.J. (登録日: 2016-07-19, 公開日: 2016-10-12, 最終更新日: 2024-05-08)

主引用文献

Iadanza, M.G.,Higgins, A.J.,Schiffrin, B.,Calabrese, A.N.,Brockwell, D.J.,Ashcroft, A.E.,Radford, S.E.,Ranson, N.A.
Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM.
Nat Commun, 7:12865-12865, 2016

PubMed Abstract: The β-barrel assembly machinery (BAM) is a ∼203 kDa complex of five proteins (BamA-E), which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel proteins into the outer membrane via a poorly understood mechanism. Several current models suggest that BAM functions through a 'lateral gating' motion of the β-barrel of BamA. Here we present a cryo-EM structure of the BamABCDE complex, at 4.9 Å resolution. The structure is in a laterally open conformation showing that gating is independent of BamB binding. We describe conformational changes throughout the complex and interactions between BamA, B, D and E, and the detergent micelle that suggest communication between BAM and the lipid bilayer. Finally, using an enhanced reconstitution protocol and functional assays, we show that for the outer membrane protein OmpT, efficient folding in vitro requires lateral gating in BAM.

PubMed: 27686148
DOI: 10.1038/ncomms12865

実験手法

ELECTRON MICROSCOPY (4.9 Å)