9FUR

MsbA in LMNG inward-facing narrow

9FUR の概要

• エントリーDOI: 10.2210/pdb9fur/pdb
• EMDBエントリー: 50775
• 分子名称: ATP-dependent lipid A-core flippase, (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-5-[(2~{S},3~{S},4~{R},5~{R},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{R},5~{S},6~{R})-6-[(1~{S})-2-[(2~{S},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-1-oxidanyl-ethyl]-3,4-bis(oxidanyl)-5-phosphonooxy-oxan-2-yl]oxy-3-oxidanyl-5-phosphonooxy-oxan-2-yl]oxy-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid (2 entities in total)
• 機能のキーワード: abc transporter, transport protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 132036.26

構造登録者

Hoffmann, L.,Baier, A.,Jorde, L.,Kamel, M.,Schaefer, J.,Schnelle, K.,Scholz, A.,Shvarev, D.,Wong, J.,Parey, K.,Januliene, D.,Moeller, A. (登録日: 2024-06-26, 公開日: 2025-03-19, 最終更新日: 2025-05-14)

主引用文献

Hoffmann, L.,Baier, A.,Jorde, L.,Kamel, M.,Schafer, J.H.,Schnelle, K.,Scholz, A.,Shvarev, D.,Wong, J.E.M.M.,Parey, K.,Januliene, D.,Moeller, A.
The ABC transporter MsbA in a dozen environments.
Structure, 33:916-, 2025

PubMed Abstract: High-resolution structure determination of membrane proteins typically requires reconstitution into artificial membrane mimics. The choice of the specific membrane substitute can strongly affect the protein's specific activity, stability, and conformational spectrum, potentially leading to errors or misinterpretation during analysis. The bacterial ATP-binding cassette transporter MsbA is a prominent example of such environment-specific bias. Here, we present a systematic analysis of the conformational spectrum of MsbA, stabilized in a dozen environments, using cryoelectron microscopy (cryo-EM), and show pronounced feedback between the membrane mimetics and the transporter. Detergents generally favor wide inward-facing conformations while nanodiscs induce narrower conformations. Notably, only in three tested environments, MsbA samples the full movement of the nucleotide-binding domains, including narrow and wide conformations. We expect this study to serve as a blueprint for other membrane proteins, even where a structural reaction to the hydrophobic environment is not directly visible but still critical for the proteins' function.

PubMed: 40056915
DOI: 10.1016/j.str.2025.02.002

実験手法

ELECTRON MICROSCOPY (3.8 Å)