7RR6

Multidrug efflux pump subunit AcrB

7RR6 の概要

• エントリーDOI: 10.2210/pdb7rr6/pdb
• EMDBエントリー: 24653 24654 24655
• 分子名称: Multidrug efflux pump subunit AcrB, PHOSPHATIDYLETHANOLAMINE, DODECANE (3 entities in total)
• 機能のキーワード: multidrug efflux pump subunit acrb, ncmn, transport protein
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 365390.60

構造登録者

Trinh, T.K.H.,Cabezas, A.,Catalano, C.,Qiu, W.,des Georges, A.,Guo, Y. (登録日: 2021-08-09, 公開日: 2022-08-17, 最終更新日: 2024-10-23)

主引用文献

Trinh, T.K.H.,Cabezas, A.J.,Joshi, S.,Catalano, C.,Siddique, A.B.,Qiu, W.,Deshmukh, S.,des Georges, A.,Guo, Y.
pH-tunable membrane-active polymers, NCMNP2a- x , and their potential membrane protein applications.
Chem Sci, 14:7310-7326, 2023

PubMed Abstract: Accurate 3D structures of membrane proteins are essential for comprehending their mechanisms of action and designing specific ligands to modulate their activities. However, these structures are still uncommon due to the involvement of detergents in the sample preparation. Recently, membrane-active polymers have emerged as an alternative to detergents, but their incompatibility with low pH and divalent cations has hindered their efficacy. Herein, we describe the design, synthesis, characterization, and application of a new class of pH-tunable membrane-active polymers, NCMNP2a-. The results demonstrated that NCMNP2a- could be used for high-resolution single-particle cryo-EM structural analysis of AcrB in various pH conditions and can effectively solubilize TSPO with the function preserved. Molecular dynamic simulation is consistent with experimental data that shed great insights into the working mechanism of this class of polymers. These results demonstrated that NCMNP2a- might have broad applications in membrane protein research.

PubMed: 37416719
DOI: 10.1039/d3sc01890c

実験手法

ELECTRON MICROSCOPY (3.1 Å)