In this section
@article{Low:2014:10.1038/nature13081,
author = {Low, HH and Gubellini, F and Rivera-Calzada, A and Braun, N and Connery, S and Dujeancourt, A and Lu, F and Redzej, A and Fronzes, R and Orlova, EV and Waksman, G},
doi = {10.1038/nature13081},
journal = {Nature},
pages = {550--553},
title = {Structure of a Type IV secretion system},
url = {http://dx.doi.org/10.1038/nature13081},
volume = {508},
year = {2014}
}
TY - JOUR
AB - Bacterial type IV secretion systems translocate virulence factors into eukaryotic cells1,2, distribute genetic material between bacteria and have shown potential as a tool for the genetic modification of human cells3. Given the complex choreography of the substrate through the secretion apparatus4, the molecular mechanism of the type IV secretion system has proved difficult to dissect in the absence of structural data for the entire machinery. Here we use electron microscopy to reconstruct the type IV secretion system encoded by the Escherichia coli R388 conjugative plasmid. We show that eight proteins assemble in an intricate stoichiometric relationship to form an approximately 3 megadalton nanomachine that spans the entire cell envelope. The structure comprises an outer membrane-associated core complex1 connected by a central stalk to a substantial inner membrane complex that is dominated by a battery of 12 VirB4 ATPase subunits organized as side-by-side hexameric barrels. Our results show a secretion system with markedly different architecture, and consequently mechanism, to other known bacterial secretion systems1,4,5,6.
AU - Low,HH
AU - Gubellini,F
AU - Rivera-Calzada,A
AU - Braun,N
AU - Connery,S
AU - Dujeancourt,A
AU - Lu,F
AU - Redzej,A
AU - Fronzes,R
AU - Orlova,EV
AU - Waksman,G
DO - 10.1038/nature13081
EP - 553
PY - 2014///
SN - 0028-0836
SP - 550
TI - Structure of a Type IV secretion system
T2 - Nature
UR - http://dx.doi.org/10.1038/nature13081
UR - https://www.nature.com/articles/nature13081
VL - 508
ER -
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