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TitleStructures of the wild-type MexAB-OprM tripartite pump reveal its complex formation and drug efflux mechanism.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 1520, Year 2019
Publish dateApr 3, 2019
AuthorsKenta Tsutsumi / Ryo Yonehara / Etsuko Ishizaka-Ikeda / Naoyuki Miyazaki / Shintaro Maeda / Kenji Iwasaki / Atsushi Nakagawa / Eiki Yamashita /
PubMed AbstractIn Pseudomonas aeruginosa, MexAB-OprM plays a central role in multidrug resistance by ejecting various drug compounds, which is one of the causes of serious nosocomial infections. Although the ...In Pseudomonas aeruginosa, MexAB-OprM plays a central role in multidrug resistance by ejecting various drug compounds, which is one of the causes of serious nosocomial infections. Although the structures of the components of MexAB-OprM have been solved individually by X-ray crystallography, no structural information for fully assembled pumps from P. aeruginosa were previously available. In this study, we present the structure of wild-type MexAB-OprM in the presence or absence of drugs at near-atomic resolution. The structure reveals that OprM does not interact with MexB directly, and that it opens its periplasmic gate by forming a complex. Furthermore, we confirm the residues essential for complex formation and observed a movement of the drug entrance gate. Based on these results, we propose mechanisms for complex formation and drug efflux.
External linksNat Commun / PubMed:30944318 / PubMed Central
MethodsEM (single particle)
Resolution3.64 - 3.76 Å
Structure data

9695

6iok

EMDB-9695, PDB-6iok:
Cryo-EM structure of multidrug efflux pump MexAB-OprM (0 degree state)
Method: EM (single particle) / Resolution: 3.64 Å

9696

6iol

EMDB-9696, PDB-6iol:
Cryo-EM structure of multidrug efflux pump MexAB-OprM (60 degree state)
Method: EM (single particle) / Resolution: 3.76 Å

Source
  • pseudomonas aeruginosa (bacteria)
  • pseudomonas aeruginosa pao1 (bacteria)
KeywordsMEMBRANE PROTEIN / Multidrug resistance / efflux / complex

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