| Literature DB >> 25818299 |
Chih-Chia Su1, Jani Reddy Bolla2, Nitin Kumar2, Abhijith Radhakrishnan2, Feng Long1, Jared A Delmar1, Tsung-Han Chou1, Kanagalaghatta R Rajashankar3, William M Shafer4, Edward W Yu5.
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. N. gonorrhoeae MtrF is an integral membrane protein that belongs to the AbgT family of transporters for which no structural information is available. Here, we describe the crystal structure of MtrF, revealing a dimeric molecule with architecture distinct from all other families of transporters. MtrF is a bowl-shaped dimer with a solvent-filled basin extending from the cytoplasm to halfway across the membrane bilayer. Each subunit of the transporter contains nine transmembrane helices and two hairpins, posing a plausible pathway for substrate transport. A combination of the crystal structure and biochemical functional assays suggests that MtrF is an antibiotic efflux pump mediating bacterial resistance to sulfonamide antimetabolite drugs.Entities:
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Year: 2015 PMID： 25818299 PMCID： PMC4410016 DOI： 10.1016/j.celrep.2015.03.003
Source DB: PubMed Journal: Cell Rep Impact factor: 9.423