6XBD

Cryo-EM structure of MlaFEDB in nanodiscs with phospholipid substrates

6XBD の概要

• エントリーDOI: 10.2210/pdb6xbd/pdb
• EMDBエントリー: 22116
• 分子名称: Phospholipid ABC transporter-binding protein MlaD, Phospholipid ABC transporter permease protein MlaE, Phospholipid transport system ATP-binding protein MlaF, ... (6 entities in total)
• 機能のキーワード: lipid transport, bacterial cell envelope, mla pathway, mce
• 由来する生物種: Escherichia coli DEC6A; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 296368.94

構造登録者

Coudray, N.,Isom, G.L.,MacRae, M.R.,Saiduddin, M.,Ekiert, D.C.,Bhabha, G. (登録日: 2020-06-05, 公開日: 2020-07-01, 最終更新日: 2024-03-06)

主引用文献

Coudray, N.,Isom, G.L.,MacRae, M.R.,Saiduddin, M.N.,Bhabha, G.,Ekiert, D.C.
Structure of bacterial phospholipid transporter MlaFEDB with substrate bound.
Elife, 9:-, 2020

PubMed Abstract: In double-membraned bacteria, phospholipid transport across the cell envelope is critical to maintain the outer membrane barrier, which plays a key role in virulence and antibiotic resistance. An MCE transport system called Mla has been implicated in phospholipid trafficking and outer membrane integrity, and includes an ABC transporter, MlaFEDB. The transmembrane subunit, MlaE, has minimal sequence similarity to other transporters, and the structure of the entire inner-membrane MlaFEDB complex remains unknown. Here, we report the cryo-EM structure of MlaFEDB at 3.05 Å resolution, revealing distant relationships to the LPS and MacAB transporters, as well as the eukaryotic ABCA/ABCG families. A continuous transport pathway extends from the MlaE substrate-binding site, through the channel of MlaD, and into the periplasm. Unexpectedly, two phospholipids are bound to MlaFEDB, suggesting that multiple lipid substrates may be transported each cycle. Our structure provides mechanistic insight into substrate recognition and transport by MlaFEDB.

PubMed: 33236984
DOI: 10.7554/eLife.62518

実験手法

ELECTRON MICROSCOPY (3.05 Å)