title: Crystal structure of the open state of the Neisseria gonorrhoeae MtrE outer membrane channel.
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.
authors.affiliation: Department of Chemistry, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Hsiang-Ting
authors.initials: HT
authors.lastname: Lei
authors.affiliation: Department of Physics and Astronomy, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Tsung-Han
authors.initials: TH
authors.lastname: Chou
authors.affiliation: Department of Physics and Astronomy, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Chih-Chia
authors.initials: CC
authors.lastname: Su
authors.affiliation: Department of Chemistry, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Jani Reddy
authors.initials: JR
authors.lastname: Bolla
authors.affiliation: Department of Chemistry, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Nitin
authors.initials: N
authors.lastname: Kumar
authors.affiliation: Department of Chemistry, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Abhijith
authors.initials: A
authors.lastname: Radhakrishnan
authors.affiliation: Department of Chemistry, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Feng
authors.initials: F
authors.lastname: Long
authors.affiliation: Department of Physics and Astronomy, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Jared A
authors.initials: JA
authors.lastname: Delmar
authors.affiliation: Bioinformatics and Computational Biology Interdepartmental Graduate Program, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Sylvia V
authors.initials: SV
authors.lastname: Do
authors.affiliation: NE-CAT and Department of Chemistry and Chemical Biology, Cornell University, Argonne National Laboratory, Argonne, Illinois, United States of America.
authors.forename: Kanagalaghatta R
authors.initials: KR
authors.lastname: Rajashankar
authors.affiliation: Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia, United States of America; Laboratories of Microbial Pathogenesis, VA Medical Center, Decatur, Georgia, United States of America.
authors.forename: William M
authors.initials: WM
authors.lastname: Shafer
authors.affiliation: Department of Chemistry, Iowa State University, Ames, Iowa, United States of America; Department of Physics and Astronomy, Iowa State University, Ames, Iowa, United States of America; Bioinformatics and Computational Biology Interdepartmental Graduate Program, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Edward W
authors.initials: EW
authors.lastname: Yu
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D009344:Neisseria gonorrhoeae / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D001425:Bacterial Outer Membrane Proteins; C107796:MtrE protein, Neisseria gonorrhoeae