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Structure of the bacterial sex F pilus reveals an assembly of a stoichiometric protein-phospholipid complex
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dc.contributor.author | Costa, Tiago R. D. | |
dc.contributor.author | langovan, Aravindan I | |
dc.contributor.author | Ukleja, Marta | |
dc.contributor.author | Redjez, Adam | |
dc.contributor.author | Santini, Joanne M. | |
dc.contributor.author | Smith, Terry K. | |
dc.contributor.author | Egelman, Edward H. | |
dc.contributor.author | Waksman, Gabriel | |
dc.date.accessioned | 2016-09-09T10:30:10Z | |
dc.date.available | 2016-09-09T10:30:10Z | |
dc.date.issued | 2016-09-08 | |
dc.identifier.citation | Costa , T R D , langovan , A I , Ukleja , M , Redjez , A , Santini , J M , Smith , T K , Egelman , E H & Waksman , G 2016 , ' Structure of the bacterial sex F pilus reveals an assembly of a stoichiometric protein-phospholipid complex ' , Cell , vol. 166 , no. 6 , e10 , pp. 1436-1444 . https://doi.org/10.1016/j.cell.2016.08.025 | en |
dc.identifier.issn | 0092-8674 | |
dc.identifier.other | PURE: 244482702 | |
dc.identifier.other | PURE UUID: 395bf38f-3e54-490a-94b3-b779ac838f2b | |
dc.identifier.other | Scopus: 84986294152 | |
dc.identifier.other | WOS: 000386339900016 | |
dc.identifier.uri | https://hdl.handle.net/10023/9465 | |
dc.description | This work was supported by Wellcome Trust grants 098302 to G.W. and 093228 to T.K.S. and NIH grant GM035269 to E.H.E. | en |
dc.description.abstract | Conjugative pili are widespread bacterial appendages that play important roles in horizontal gene transfer, in spread of antibiotic resistance genes, and as sites of phage attachment. Among conjugative pili, the F “sex” pilus encoded by the F plasmid is the best functionally characterized, and it is also historically the most important, as the discovery of F-plasmid-mediated conjugation ushered in the era of molecular biology and genetics. Yet, its structure is unknown. Here, we present atomic models of two F family pili, the F and pED208 pili, generated from cryoelectron microscopy reconstructions at 5.0 and 3.6 Å resolution, respectively. These structures reveal that conjugative pili are assemblies of stoichiometric protein-phospholipid units. We further demonstrate that each pilus type binds preferentially to particular phospholipids. These structures provide the molecular basis for F pilus assembly and also shed light on the remarkable properties of conjugative pili in bacterial secretion and phage infection. | |
dc.format.extent | 20 | |
dc.language.iso | eng | |
dc.relation.ispartof | Cell | en |
dc.rights | Copyright: 2016 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.subject | Pilus | en |
dc.subject | Conjugation | en |
dc.subject | Type 4 Secretion System | en |
dc.subject | Phospholipid | en |
dc.subject | Protein-phospholipid complex | en |
dc.subject | Structural biology | en |
dc.subject | Cryoelectron Microscopy | en |
dc.subject | QH301 Biology | en |
dc.subject | DAS | en |
dc.subject.lcc | QH301 | en |
dc.title | Structure of the bacterial sex F pilus reveals an assembly of a stoichiometric protein-phospholipid complex | en |
dc.type | Journal article | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | https://doi.org/10.1016/j.cell.2016.08.025 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | 093228/Z/10/Z | en |
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