title: Crystal structure of the Neisseria gonorrhoeae MtrD inner membrane multidrug efflux pump.
abstract: Neisseria gonorrhoeae is an obligate human pathogen and the causative agent of the sexually-transmitted disease gonorrhea. The control of this disease has been compromised by the increasing proportion of infections due to antibiotic-resistant strains, which are growing at an alarming rate. The 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 report the crystal structure of the inner membrane MtrD multidrug efflux pump, which reveals a novel structural feature that is not found in other RND efflux pumps.
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 Physics and Astronomy, Iowa State University, Ames, Iowa, United States of America.
authors.forename: Chih-Chia
authors.initials: CC
authors.lastname: Su
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: 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: Nitin
authors.initials: N
authors.lastname: Kumar
authors.affiliation: Department of Physics and Astronomy, 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: 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: Jared A
authors.initials: JA
authors.lastname: Delmar
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: 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: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008565:Membrane Proteins / Q000737:chemistry*; D026901:Membrane Transport Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009344:Neisseria gonorrhoeae / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; C107795:MtrD protein, Neisseria gonorrhoeae