Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD

被引:119
作者
Johnson, Steven
Roversi, Pietro
Espina, Marianela
Olive, Andrew
Deane, Janet E.
Birket, Susan
Field, Terry
Picking, William D.
Blocker, Ariel J.
Galyov, Edouard E.
Picking, Wendy L.
Lea, Susan M.
机构
[1] Univ Oxford, Dept Biochem, Mol Biophys Lab, Oxford OX1 3QU, England
[2] Univ Oxford, Sir William Dunn Sch Pathol, Oxford OX1 3RE, England
[3] Univ Kansas, Dept Mol Biosci, Lawrence, KS 66045 USA
[4] Inst Anim Hlth, Div Microbiol, Compton Lab, Compton RG20 7NN, Berks, England
基金
英国医学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
D O I
10.1074/jbc.M607945200
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
Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle through which effector proteins are secreted. We report multiple crystal structures of two proteins that sit at the tip of the needle and are essential for virulence: IpaD from Shigella flexneri and BipD from Burkholderia pseudomallei. The structures reveal that the N-terminal domains of the molecules are intramolecular chaperones that prevent premature oligomerization, as well as sharing structural homology with proteins involved in eukaryotic actin rearrangement. Crystal packing has allowed us to construct a model for the tip complex that is supported by mutations designed using the structure.
引用
收藏
页码:4035 / 4044
页数:10
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