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dc.contributor.authorIlangovan, Aravindan
dc.contributor.authorKay, Christopher W. M.
dc.contributor.authorRoier, Sandro
dc.contributor.authorEl Mkami, Hassane
dc.contributor.authorSalvadori, Enrico
dc.contributor.authorZechner, Ellen L.
dc.contributor.authorZanetti, Giulia
dc.contributor.authorWaksman, Gabriel
dc.date.accessioned2017-05-09T16:30:12Z
dc.date.available2017-05-09T16:30:12Z
dc.date.issued2017-05-04
dc.identifier.citationIlangovan , A , Kay , C W M , Roier , S , El Mkami , H , Salvadori , E , Zechner , E L , Zanetti , G & Waksman , G 2017 , ' Cryo-EM structure of a relaxase reveals the molecular basis of DNA unwinding during bacterial conjugation ' Cell , vol 169 , no. 4 , e12 , pp. 708-721 . DOI: 10.1016/j.cell.2017.04.010en
dc.identifier.issn0092-8674
dc.identifier.otherPURE: 249879386
dc.identifier.otherPURE UUID: 3fc54b3c-5f5e-49c9-92b1-7b444ffe60ec
dc.identifier.otherRIS: urn:2D5EDA48F4C8F4C403B0C63CD59F0545
dc.identifier.otherScopus: 85018171488
dc.identifier.urihttp://hdl.handle.net/10023/10733
dc.identifier.urihttp://www.sciencedirect.com/science/article/pii/S0092867417304233#appd002en
dc.descriptionThis work was supported by Wellcome Trust grant 098302 to G.W., a Royal Society Dorothy Hodgkin fellowship to G.Z. DH130048, and Austrian Science Fund (FWF) grants P24016 and W901 DK Molecular Enzymology to E.L.Z. S.R. is a BioTechMed-Graz PostDoc. H.E.M. and the EPR Facility at St Andrews are supported in part by Wellcome Trust grant 099149/Z/12/Z.en
dc.description.abstractRelaxases play essential roles in conjugation, the main process by which bacteria exchange genetic material, notably antibiotic resistance genes. They are bifunctional enzymes containing a trans-esterase activity, which is responsible for nicking the DNA strand to be transferred and for covalent attachment to the resulting 5′-phosphate end, and a helicase activity, which is responsible for unwinding the DNA while it is being transported to a recipient cell. Here we show that these two activities are carried out by two conformers that can both load simultaneously on the origin of transfer DNA. We solve the structure of one of these conformers by cryo electron microscopy to near-atomic resolution, elucidating the molecular basis of helicase function by relaxases and revealing insights into the mechanistic events taking place in the cell prior to substrate transport during conjugation.en
dc.format.extent27en
dc.language.isoeng
dc.relation.ispartofCellen
dc.rights© 2017 The Author(s). Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).en
dc.subjectRelaxaseen
dc.subjectTraIen
dc.subjectBacterial conjugationen
dc.subjectCryo-electron microscopyen
dc.subjectType IV secretion systemen
dc.subjectStructural biologyen
dc.subjectQH301 Biologyen
dc.subjectDASen
dc.subject.lccQH301en
dc.titleCryo-EM structure of a relaxase reveals the molecular basis of DNA unwinding during bacterial conjugationen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Physics and Astronomyen
dc.identifier.doihttp://dx.doi.org/10.1016/j.cell.2017.04.010
dc.description.statusPeer revieweden


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