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

被引：70
|
作者：
Rivera-Calzada, Angel [1 ,2 ]
Fronzes, Remi [3 ]
Savva, Christos G. [1 ,2 ]
Chandran, Vidya [1 ,2 ]
Lian, Pei W. [1 ,2 ]
Laeremans, Toon [4 ,5 ]
Pardon, Els [4 ,5 ]
Steyaert, Jan [4 ,5 ]
Remaut, Han [4 ,5 ]
Waksman, Gabriel [1 ,2 ]
Orlova, Elena V. [1 ,2 ]
机构：
[1] UCL, Dept Biol Sci, Inst Struct & Mol Biol, London WC1E 7HX, England
[2] Birkbeck, London WC1E 7HX, England
[3] Inst Pasteur, UMR CNRS 3528, Paris, France
[4] Vrije Univ Brussel, Struct Biol Brussels, Brussels, Belgium
[5] Vlaams Inst Biotechnol, Dept Biol Struct, Brussels, Belgium
来源：
EMBO JOURNAL | 2013年 / 32卷 / 08期
基金：
英国惠康基金;
关键词：
core complex; cryo electron microscopy; pKM101; structure; type 4 secretion system; PROTEIN-STRUCTURE; AGROBACTERIUM VIRB10; STRUCTURE PREDICTION; DNA TRANSFER; CONJUGATION; DIVERSITY; SYSTEM; ATPASE; BSOFT; IMAGE;
D O I：
10.1038/emboj.2013.58
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. The EMBO Journal (2013) 32, 1195-1204. doi: 10.1038/emboj.2013.58; Published online 19 March 2013
引用
收藏
页码：1195 / 1204
页数：10
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