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.
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.
Copyright Date
2015
Language
en
File Format
application/pdf
Recommended Citation
Su, Chih-Chia; Bolla, Jani Reddy; Kumar, Nitin; Radhakrishnan, Pattathil; Long, Feng; Delmar, Jared A.; Chou, Tsung-Han; Rajashankar, Kanagalaghatta R.; Shafer, William M.; and Yu, Edward, "Structure and Function of Neisseria gonorrhoeae MtrF Illuminates a Class of Antimetabolite Efflux Pumps" (2015). Physics and Astronomy Publications. 167.
https://lib.dr.iastate.edu/physastro_pubs/167
Included in
Biological and Chemical Physics Commons, Medicinal-Pharmaceutical Chemistry Commons, Other Chemistry Commons, Other Physics Commons
Comments
This article is from Cell Reports 11 (2015): 61, doi:10.1016/j.celrep.2015.03.003. Posted with permission.