6QWR

Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers

6QWR の概要

• エントリーDOI: 10.2210/pdb6qwr/pdb
• 関連するPDBエントリー: 6QAM
• NMR情報: BMRB: 34365
• 分子名称: Outer membrane protein AlkL (1 entity in total)
• 機能のキーワード: outer membrane protein, beta barrel, porin, transporter, membrane protein
• 由来する生物種: Pseudomonas oleovorans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24087.91

構造登録者

Schubeis, T.,Andreas, L.B.,Pintacuda, G. (登録日: 2019-03-06, 公開日: 2020-03-18, 最終更新日: 2024-06-19)

主引用文献

Schubeis, T.,Le Marchand, T.,Daday, C.,Kopec, W.,Tekwani Movellan, K.,Stanek, J.,Schwarzer, T.S.,Castiglione, K.,de Groot, B.L.,Pintacuda, G.,Andreas, L.B.
A beta-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL.
Proc.Natl.Acad.Sci.USA, 117:21014-21021, 2020

PubMed Abstract: The protein AlkL is known to increase permeability of the outer membrane of bacteria for hydrophobic molecules, yet the mechanism of transport has not been determined. Differing crystal and NMR structures of homologous proteins resulted in a controversy regarding the degree of structure and the role of long extracellular loops. Here we solve this controversy by determining the de novo NMR structure in near-native lipid bilayers, and by accessing structural dynamics relevant to hydrophobic substrate permeation through molecular-dynamics simulations and by characteristic NMR relaxation parameters. Dynamic lateral exit sites large enough to accommodate substrates such as carvone or octane occur through restructuring of a barrel extension formed by the extracellular loops.

PubMed: 32817429
DOI: 10.1073/pnas.2002598117

実験手法

SOLID-STATE NMR