In this section
@article{Costa:2016:10.1016/j.cell.2016.08.025,
author = {Costa, TRD and Ilangovan, A and Ukleja, M and Redzej, A and Santini, JM and Smith, TK and Egelman, EH and Waksman, G},
doi = {10.1016/j.cell.2016.08.025},
journal = {CELL},
pages = {1436--1444.e10},
title = {Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex},
url = {http://dx.doi.org/10.1016/j.cell.2016.08.025},
volume = {166},
year = {2016}
}
TY - JOUR
AB - 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.
AU - Costa,TRD
AU - Ilangovan,A
AU - Ukleja,M
AU - Redzej,A
AU - Santini,JM
AU - Smith,TK
AU - Egelman,EH
AU - Waksman,G
DO - 10.1016/j.cell.2016.08.025
EP - 1444
PY - 2016///
SN - 0092-8674
SP - 1436
TI - Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex
T2 - CELL
UR - http://dx.doi.org/10.1016/j.cell.2016.08.025
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000386339900016&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
VL - 166
ER -
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