Structure of the bacterial sex F pilus reveals an assembly of a stoichiometric protein-phospholipid complex
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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.
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 . DOI: 10.1016/j.cell.2016.08.025
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/).
DescriptionThis 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.
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