Crystal structure of the Neisseria gonorrhoeae MtrD inner membrane multidrug efflux pump

PLoS One. 2014 Jun 5;9(6):e97903. doi: 10.1371/journal.pone.0097903. eCollection 2014.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Binding Sites
  • Crystallography, X-Ray
  • Membrane Proteins / chemistry*
  • Membrane Transport Proteins / chemistry*
  • Models, Molecular*
  • Molecular Sequence Data
  • Neisseria gonorrhoeae / metabolism*
  • Protein Binding
  • Protein Conformation*
  • Sequence Alignment

Substances

  • Bacterial Proteins
  • Membrane Proteins
  • Membrane Transport Proteins
  • MtrD protein, Neisseria gonorrhoeae

Associated data

  • PDB/4MT1