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5AYW

Structure of a membrane complex

5AYW の概要
エントリーDOI10.2210/pdb5ayw/pdb
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membrane protein, complex, membrane biogenesis
由来する生物種Escherichia coli (strain K12)
詳細
細胞内の位置Cell outer membrane : P0A940
Cell outer membrane ; Lipid-anchor : P77774 P0A903 P0AC02 P0A937
タンパク質・核酸の鎖数5
化学式量合計172548.46
構造登録者
Huang, Y.,Han, L.,Zheng, J. (登録日: 2015-09-14, 公開日: 2016-02-24, 最終更新日: 2024-03-20)
主引用文献Han, L.,Zheng, J.,Wang, Y.,Yang, X.,Liu, Y.,Sun, C.,Cao, B.,Zhou, H.,Ni, D.,Lou, J.,Zhao, Y.,Huang, Y.
Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins
Nat.Struct.Mol.Biol., 23:192-196, 2016
Cited by
PubMed Abstract: In Gram-negative bacteria, the assembly of β-barrel outer-membrane proteins (OMPs) requires the β-barrel-assembly machinery (BAM) complex. We determined the crystal structure of the 200-kDa BAM complex from Escherichia coli at 3.55-Å resolution. The structure revealed that the BAM complex assembles into a hat-like shape, in which the BamA β-barrel domain forms the hat's crown embedded in the outer membrane, and its five polypeptide transport-associated (POTRA) domains interact with the four lipoproteins BamB, BamC, BamD and BamE, thus forming the hat's brim in the periplasm. The assembly of the BAM complex creates a ring-like apparatus beneath the BamA β-barrel in the periplasm and a potential substrate-exit pore located at the outer membrane-periplasm interface. The complex structure suggests that the chaperone-bound OMP substrates may feed into the chamber of the ring-like apparatus and insert into the outer membrane via the potential substrate-exit pore in an energy-independent manner.
PubMed: 26900875
DOI: 10.1038/nsmb.3181
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.555 Å)
構造検証レポート
Validation report summary of 5ayw
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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