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5UVN

Structure of E. coli MCE protein PqiB, periplasmic domain

5UVN の概要
エントリーDOI10.2210/pdb5uvn/pdb
関連するPDBエントリー5UW2 5UW8 5UWA
EMDBエントリー8608 8611 8612
分子名称Paraquat-inducible protein B (1 entity in total)
機能のキーワードmce protein, bacterial lipid transport, transport protein
由来する生物種Escherichia coli
詳細
タンパク質・核酸の鎖数6
化学式量合計293142.26
構造登録者
Bhabha, G.,Ekiert, D.C. (登録日: 2017-02-20, 公開日: 2017-04-12, 最終更新日: 2024-03-13)
主引用文献Ekiert, D.C.,Bhabha, G.,Isom, G.L.,Greenan, G.,Ovchinnikov, S.,Henderson, I.R.,Cox, J.S.,Vale, R.D.
Architectures of Lipid Transport Systems for the Bacterial Outer Membrane.
Cell, 169:273-285.e17, 2017
Cited by
PubMed Abstract: How phospholipids are trafficked between the bacterial inner and outer membranes through the hydrophilic space of the periplasm is not known. We report that members of the mammalian cell entry (MCE) protein family form hexameric assemblies with a central channel capable of mediating lipid transport. The E. coli MCE protein, MlaD, forms a ring associated with an ABC transporter complex in the inner membrane. A soluble lipid-binding protein, MlaC, ferries lipids between MlaD and an outer membrane protein complex. In contrast, EM structures of two other E. coli MCE proteins show that YebT forms an elongated tube consisting of seven stacked MCE rings, and PqiB adopts a syringe-like architecture. Both YebT and PqiB create channels of sufficient length to span the periplasmic space. This work reveals diverse architectures of highly conserved protein-based channels implicated in the transport of lipids between the membranes of bacteria and some eukaryotic organelles.
PubMed: 28388411
DOI: 10.1016/j.cell.2017.03.019
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.96 Å)
構造検証レポート
Validation report summary of 5uvn
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2025-12-31に公開中

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