7RR6

Multidrug efflux pump subunit AcrB

Summary for 7RR6

• Entry DOI: 10.2210/pdb7rr6/pdb
• EMDB information: 24653 24654 24655
• Descriptor: Multidrug efflux pump subunit AcrB, PHOSPHATIDYLETHANOLAMINE, DODECANE (3 entities in total)
• Functional Keywords: multidrug efflux pump subunit acrb, ncmn, transport protein
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 3
• Total formula weight: 365390.60

Authors

Trinh, T.K.H.,Cabezas, A.,Catalano, C.,Qiu, W.,des Georges, A.,Guo, Y. (deposition date: 2021-08-09, release date: 2022-08-17, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.1 Å)