6M96

ATP-bound conformation of the WzmWzt O antigen ABC transporter

6M96 の概要

• エントリーDOI: 10.2210/pdb6m96/pdb
• 関連するPDBエントリー: 6AN7
• 分子名称: ABC transporter, Transport permease protein, LAURYL DIMETHYLAMINE-N-OXIDE, ... (10 entities in total)
• 機能のキーワード: o antigen, channel, membrane protein, transport protein, membrane protein-transport protein complex, membrane protein/transport protein
• 由来する生物種: Aquifex aeolicus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67850.81

構造登録者

Caffalette, C.A.,Zimmer, J. (登録日: 2018-08-22, 公開日: 2019-03-06, 最終更新日: 2023-10-11)

主引用文献

Caffalette, C.A.,Corey, R.A.,Sansom, M.S.P.,Stansfeld, P.J.,Zimmer, J.
A lipid gating mechanism for the channel-forming O antigen ABC transporter.
Nat Commun, 10:824-824, 2019

PubMed Abstract: Extracellular glycan biosynthesis is a widespread microbial protection mechanism. In Gram-negative bacteria, the O antigen polysaccharide represents the variable region of outer membrane lipopolysaccharides. Fully assembled lipid-linked O antigens are translocated across the inner membrane by the WzmWzt ABC transporter for ligation to the lipopolysaccharide core, with the transporter forming a continuous transmembrane channel in a nucleotide-free state. Here, we report its structure in an ATP-bound conformation. Large structural changes within the nucleotide-binding and transmembrane regions push conserved hydrophobic residues at the substrate entry site towards the periplasm and provide a model for polysaccharide translocation. With ATP bound, the transporter forms a large transmembrane channel with openings toward the membrane and periplasm. The channel's periplasmic exit is sealed by detergent molecules that block solvent permeation. Molecular dynamics simulation data suggest that, in a biological membrane, lipid molecules occupy this periplasmic exit and prevent water flux in the transporter's resting state.

PubMed: 30778065
DOI: 10.1038/s41467-019-08646-8

実験手法

X-RAY DIFFRACTION (2.05 Å)