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Structure of a bacterial type IV secretion core complex at subnanometre resolution

Rivera-Calzada, A; Fronzes, R; Savva, CG; Chandran, V; Lian, PW; Laeremans, T; Pardon, E; ... Orlova, EV; + view all (2013) Structure of a bacterial type IV secretion core complex at subnanometre resolution. The EMBO Journal , 32 (8) 1195 -1204. 10.1038/emboj.2013.58. Green open access

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Abstract

Type IV secretion (T4S) systems are able to transport DNAs and/or proteins through the membranes of bacteria. They form large multiprotein complexes consisting of 12 proteins termed VirB1-11 and VirD4. VirB7, 9 and 10 assemble into a 1.07 MegaDalton membrane-spanning core complex (CC), around which all other components assemble. This complex is made of two parts, the O-layer inserted in the outer membrane and the I-layer inserted in the inner membrane. While the structure of the O-layer has been solved by X-ray crystallography, there is no detailed structural information on the I-layer. Using high-resolution cryo-electron microscopy and molecular modelling combined with biochemical approaches, we determined the I-layer structure and located its various components in the electron density. Our results provide new structural insights on the CC, from which the essential features of T4S system mechanisms can be derived.

Type: Article
Title: Structure of a bacterial type IV secretion core complex at subnanometre resolution
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1038/emboj.2013.58
Publisher version: http://dx.doi.org/10.1038/emboj.2013.58
Language: English
Additional information: This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. PMCID: PMC3630358
Keywords: Agrobacterium tumefaciens, Bacterial secretion systems, Cryoelectron microscopy, Membrane transport proteins, Models, Molecular, Multiprotein complexes, Protein conformation
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/1393244
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