7PH2

Nanodisc reconstituted MsbA in complex with nanobodies, spin-labeled at position A60C

7PH2 の概要

• エントリーDOI: 10.2210/pdb7ph2/pdb
• EMDBエントリー: 13404
• 分子名称: ATP-dependent lipid A-core flippase, Nb_MsbA#1, (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{S},5~{R},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,5-bis(oxidanyl)oxan-2-yl]oxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-4-[(3~{R})-3-nonanoyloxytetradecanoyl]oxy-5-[[(3~{R})-3-octanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{S},5~{S},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanylnonanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-oxan-2-yl]methoxy]-5-oxidanyl-oxane-2-carboxylic acid, ... (5 entities in total)
• 機能のキーワード: abc transporter, nanobody, gd-dota, membrane protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 159831.51

構造登録者

Januliene, D.,Parey, K.,Galazzo, L.,Meier, G.,Vecchis, D.,Striednig, B.,Hilbi, H.,Schaefer, L.V.,Kuprov, I.,Bordignon, E.,Seeger, M.A.,Moeller, A. (登録日: 2021-08-16, 公開日: 2022-08-24, 最終更新日: 2025-07-09)

主引用文献

Galazzo, L.,Meier, G.,Januliene, D.,Parey, K.,De Vecchis, D.,Striednig, B.,Hilbi, H.,Schafer, L.V.,Kuprov, I.,Moeller, A.,Bordignon, E.,Seeger, M.A.
The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells.
Sci Adv, 8:eabn6845-eabn6845, 2022

PubMed Abstract: Membrane proteins are currently investigated after detergent extraction from native cellular membranes and reconstitution into artificial liposomes or nanodiscs, thereby removing them from their physiological environment. However, to truly understand the biophysical properties of membrane proteins in a physiological environment, they must be investigated within living cells. Here, we used a spin-labeled nanobody to interrogate the conformational cycle of the ABC transporter MsbA by double electron-electron resonance. Unexpectedly, the wide inward-open conformation of MsbA, commonly considered a nonphysiological state, was found to be prominently populated in cells. Molecular dynamics simulations revealed that extensive lateral portal opening is essential to provide access of its large natural substrate core lipid A to the binding cavity. Our work paves the way to investigate the conformational landscape of membrane proteins in cells.

PubMed: 36223470
DOI: 10.1126/sciadv.abn6845

実験手法

ELECTRON MICROSCOPY (3.7 Å)