{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Su CC"],"funding":["National Institutes of General Medical Sciences","U.S. Department of Energy, Office of Basic Energy Sciences","Medical Research Service of the Department of Veterans Affairs","NIAID NIH HHS","NIH","NIGMS NIH HHS"],"pagination":["61-70"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4410016"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_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, po"],"journal":["Cell reports"],"pubmed_title":["Structure and function of Neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps."],"pmcid":["PMC4410016"],"funding_grant_id":["R37 AI021150","R37AI021150","GM103403","DE-AC02-06CH11357","R01GM086431","R01 GM086431","P41 GM103403"],"pubmed_authors":["Rajashankar KR","Long F","Chou TH","Delmar JA","Shafer WM","Su CC","Radhakrishnan A","Kumar N","Yu EW","Bolla JR"],"additional_accession":[]},"is_claimable":false,"name":"Structure and function of Neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps.","description":"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, po","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Apr","modification":"2026-05-02T01:20:05.335Z","creation":"2019-03-27T01:50:32Z"},"accession":"S-EPMC4410016","cross_references":{"pubmed":["25818299"],"doi":["10.1016/j.celrep.2015.03.003"]}}