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dc.contributor.authorDu, Dijunen
dc.contributor.authorvan, Veen Hendrik Wen
dc.contributor.authorMurakami, Satoshien
dc.contributor.authorPos, Klaas Men
dc.contributor.authorLuisi, Benen
dc.date.accessioned2015-08-28T10:12:50Z
dc.date.available2015-08-28T10:12:50Z
dc.date.issued2015-08-15en
dc.identifier.citationCurrent Opinion in Structural Biology 2015, 33:76–91. doi:10.1016/j.sbi.2015.07.015en
dc.identifier.issn0959-440X
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/250387
dc.description.abstractCells from all domains of life encode energy-dependent trans-membrane transporters that can expel harmful substances including clinically applied therapeutic agents. As a collective body, these transporters perform as a super-system that confers tolerance to an enormous range of harmful compounds and consequently aid survival in hazardous environments. In the Gram-negative bacteria, some of these transporters serve as energy-transducing components of tripartite assemblies that actively efflux drugs and other harmful compounds, as well as deliver virulence agents across the entire cell envelope. We draw together recent structural and functional data to present the current models for the transport mechanisms for the main classes of multi-drug transporters and their higher-order assemblies.
dc.description.sponsorshipBL and DD are supported by the Medical Research Council (MRC), Human Frontiers Science Program (HFSP), and the Wellcome Trust. Work in the Van Veen lab is supported by the Biotechnology and Biological Sciences Research Council (BBSRC), MRC, HFSP, Royal Society, Society for Antimicrobial Chemotherapy (BSAC), Herchel Smith Foundation, and Commonwealth Trust. Work in the Pos lab is supported by the German Research Foundation (SFB 807, Transport and Communication across Biological Membranes and FOR2251, Adaptation and persistence of the emerging pathogen Acinetobacter baumannii), the DFG-EXC115 (Cluster of Excellence Macromolecular Complexes at the Goethe-University Frankfurt), Innovative Medicines Initiative Joint Undertaking Project Translocation (IMI-Translocation), EU Marie Curie Actions ITN, HFSP and the German-Israeli Foundation (GIF). The SM laboratory is supported by ERATO Murata Lipid Active Structure Project, Japan Science and Technology Agency, the Advanced Research for Medical Products Mining Program of the National Institute of Biomedical Innovation (NIBIO) and HFSP.
dc.languageEnglishen
dc.language.isoenen
dc.publisherElsevier
dc.rightsAttribution-NonCommercial-NoDerivs 2.0 UK: England & Wales*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/2.0/uk/*
dc.titleStructure, mechanism and cooperation of bacterial multi drug transportersen
dc.typeArticle
dc.description.versionThis is the final version of the article. It first appeared from Elsevier via http://dx.doi.org/10.1016/j.sbi.2015.07.015en
prism.endingPage91
prism.publicationDate2015en
prism.publicationNameCurrent Opinion in Structural Biologyen
prism.startingPage76
prism.volume33en
dc.rioxxterms.funderWellcome Trust
dc.rioxxterms.funderBBSRC
dc.rioxxterms.funderMRC
dcterms.dateAccepted2015-07-24en
rioxxterms.versionofrecord10.1016/j.sbi.2015.07.015en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2015-08-15en
dc.contributor.orcidDu, Dijun [0000-0002-1546-8939]
dc.contributor.orcidLuisi, Ben [0000-0003-1144-9877]
dc.identifier.eissn1879-033X
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idBBSRC (BB/K017713/1)
pubs.funder-project-idMRC (MC_PC_13059)
pubs.funder-project-idHuman Frontier Science Program (HFSP) (RPG0034/2013)
pubs.funder-project-idBBSRC (BB/I002383/1)


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