Publication

Crystal Structure of the Open State of the Neisseria gonorrhoeae MtrE Outer Membrane Channel

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Last modified
  • 03/03/2025
Type of Material
Authors
    Hsiang-Ting Lei, Iowa State UniversityTsung-Han Chou, Iowa State UniversityChih-Chia Su, Iowa State UniversityJani Reddy Bolla, Iowa State UniversityNitin Kumar, Iowa State UniversityAbhijith Radhakrishnan, Iowa State UniversityFeng Long, Iowa State UniversityJared A. Delmar, Iowa State UniversitySylvia V. Do, Iowa State UniversityKanagalaghatta R. Rajashankar, Cornell UniversityWilliam Shafer, Emory UniversityEdward W. Yu, Iowa State University
Language
  • English
Date
  • 2014-06-05
Publisher
  • Public Library of Science
Publication Version
Copyright Statement
  • © 2014 Lei et al.
License
Final Published Version (URL)
Title of Journal or Parent Work
ISSN
  • 1932-6203
Volume
  • 9
Issue
  • 6
Start Page
  • e97475
End Page
  • e97475
Grant/Funding Information
  • This work is based upon research conducted at the Northeastern Collaborative Access Team beamlines of the Advanced Photon Source, supported by an award GM103403 from the National Institutes of General Medical Sciences.
  • This work was supported by NIH Grants R37AI021150 (W.M.S.) and R01GM086431 (E.W.Y.) and a VA Merit Award (W.M.S.)
Supplemental Material (URL)
Abstract
  • Active efflux of antimicrobial agents is one of the most important strategies used by bacteria to defend against antimicrobial factors present in their environment. Mediating many cases of antibiotic resistance are transmembrane efflux pumps, composed of one or more proteins. The Neisseria gonorrhoeae MtrCDE tripartite multidrug efflux pump, belonging to the hydrophobic and amphiphilic efflux resistance-nodulation-cell division (HAE-RND) family, spans both the inner and outer membranes of N. gonorrhoeae and confers resistance to a variety of antibiotics and toxic compounds. We here describe the crystal structure of N. gonorrhoeae MtrE, the outer membrane component of the MtrCDE tripartite multidrug efflux system. This trimeric MtrE channel forms a vertical tunnel extending down contiguously from the outer membrane surface to the periplasmic end, indicating that our structure of MtrE depicts an open conformational state of this channel.
Author Notes
Keywords
Research Categories
  • Biology, Molecular
  • Biology, Microbiology

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