Campus Units

Chemistry, Physics and Astronomy

Document Type

Article

Publication Version

Published Version

Publication Date

2015

Journal or Book Title

Cell Reports

Volume

11

Issue

1

First Page

61

Last Page

70

DOI

10.1016/j.celrep.2015.03.003

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.

Comments

This article is from Cell Reports 11 (2015): 61, doi:10.1016/j.celrep.2015.03.003. Posted with permission.

Rights

This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Copyright Owner

Su et al.

Language

en

File Format

application/pdf

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