2F1M

Conformational flexibility in the multidrug efflux system protein AcrA

2F1M の概要

• エントリーDOI: 10.2210/pdb2f1m/pdb
• 分子名称: Acriflavine resistance protein A (2 entities in total)
• 機能のキーワード: helical hairpin, lipoyl domain, beta barrel, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane ; Lipid- anchor : P0AE06
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 121420.74

構造登録者

Mikolosko, J.,Bobyk, K.,Zgurskaya, H.I.,Ghosh, P. (登録日: 2005-11-14, 公開日: 2006-03-21, 最終更新日: 2024-11-20)

主引用文献

Mikolosko, J.,Bobyk, K.,Zgurskaya, H.I.,Ghosh, P.
Conformational Flexibility in the Multidrug Efflux System Protein AcrA.
Structure, 14:577-587, 2006

PubMed Abstract: Intrinsic resistance to multiple drugs in many gram-negative bacterial pathogens is conferred by resistance nodulation cell division efflux pumps, which are composed of three essential components as typified by the extensively characterized Escherichia coli AcrA-AcrB-TolC system. The inner membrane drug:proton antiporter AcrB and the outer membrane channel TolC export chemically diverse compounds out of the bacterial cell, and require the activity of the third component, the periplasmic protein AcrA. The crystal structures of AcrB and TolC have previously been determined, and we complete the molecular picture of the efflux system by presenting the structure of a stable fragment of AcrA. The AcrA fragment resembles the elongated sickle shape of its homolog Pseudomonas aeruginosa MexA, being composed of three domains: beta-barrel, lipoyl, and alpha-helical hairpin. Notably, unsuspected conformational flexibility in the alpha-helical hairpin domain of AcrA is observed, which has potential mechanistic significance in coupling between AcrA conformations and TolC channel opening.

PubMed: 16531241
DOI: 10.1016/j.str.2005.11.015

実験手法

X-RAY DIFFRACTION (2.71 Å)