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TitleCryoelectron Microscopy Structures of AdeB Illuminate Mechanisms of Simultaneous Binding and Exporting of Substrates.
Journal, issue, pagesmBio, Vol. 12, Issue 1, Year 2021
Publish dateFeb 23, 2021
AuthorsChristopher E Morgan / Przemyslaw Glaza / Inga V Leus / Anhthu Trinh / Chih-Chia Su / Meng Cui / Helen I Zgurskaya / Edward W Yu /
PubMed Abstract is a Gram-negative pathogen that has emerged as one of the most highly antibiotic-resistant bacteria worldwide. Multidrug efflux within these highly drug-resistant strains and other opportunistic ... is a Gram-negative pathogen that has emerged as one of the most highly antibiotic-resistant bacteria worldwide. Multidrug efflux within these highly drug-resistant strains and other opportunistic pathogens is a major cause of failure of drug-based treatments of infectious diseases. The best-characterized multidrug efflux system in is the prevalent rug fflux B (AdeB) pump, which is a member of the resistance-nodulation-cell division (RND) superfamily. Here, we report six structures of the trimeric AdeB multidrug efflux pump in the presence of ethidium bromide using single-particle cryoelectron microscopy (cryo-EM). These structures allow us to directly observe various novel conformational states of the AdeB trimer, including the transmembrane region of trimeric AdeB can be associated with form a trimer assembly or dissociated into "dimer plus monomer" and "monomer plus monomer plus monomer" configurations. We also discover that a single AdeB protomer can simultaneously anchor a number of ethidium ligands and that different AdeB protomers can bind ethidium molecules simultaneously. Combined with molecular dynamics (MD) simulations, we reveal a drug transport mechanism that involves multiple multidrug-binding sites and various transient states of the AdeB membrane protein. Our data suggest that each AdeB protomer within the trimer binds and exports drugs independently. has emerged as one of the most highly antibiotic-resistant Gram-negative pathogens. The prevalent AdeB multidrug efflux pump mediates resistance to a broad spectrum of clinically relevant antimicrobial agents. Here, we report six cryo-EM structures of the trimeric AdeB pump in the presence of ethidium bromide. We discover that a single AdeB protomer can simultaneously anchor a number of ligands, and different AdeB protomers can bind ethidium molecules simultaneously. The results indicate that each AdeB protomer within the trimer recognizes and extrudes drugs independently.
External linksmBio / PubMed:33622726 / PubMed Central
MethodsEM (single particle)
Resolution2.97 - 3.79 Å
Structure data

22866

7kgd

EMDB-22866, PDB-7kgd:
Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-I
Method: EM (single particle) / Resolution: 3.64 Å

22867

7kge

EMDB-22867, PDB-7kge:
Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-II
Method: EM (single particle) / Resolution: 3.21 Å

22868

7kgf

EMDB-22868, PDB-7kgf:
Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-III
Method: EM (single particle) / Resolution: 3.42 Å

22869

7kgg

EMDB-22869, PDB-7kgg:
Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-ET-I
Method: EM (single particle) / Resolution: 2.97 Å

22870

7kgh

EMDB-22870, PDB-7kgh:
Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-ET-II
Method: EM (single particle) / Resolution: 3.79 Å

22871

7kgi

EMDB-22871, PDB-7kgi:
Cryo-EM Structures of AdeB from Acinetobacter baumannii: AdeB-ET-III
Method: EM (single particle) / Resolution: 3.34 Å

Chemicals

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

ChemComp-ET:
ETHIDIUM / Ethidium bromide

Source
  • acinetobacter baumannii (bacteria)
KeywordsTRANSPORT PROTEIN / AdeB / Acinetobacter baumannii / Membrane Protein / Cryo-EM / RND transporter

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