Crystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosis

被引:69
作者
Fairman, James W. [1 ]
Dautin, Nathalie [3 ]
Wojtowicz, Damian [2 ]
Liu, Wei [4 ]
Noinaj, Nicholas [1 ]
Barnard, Travis J. [1 ]
Udho, Eshwar [5 ]
Przytycka, Teresa M. [2 ]
Cherezov, Vadim [4 ]
Buchanan, Susan K. [1 ]
机构
[1] NIDDKD, Bethesda, MD 20892 USA
[2] NIH, Natl Ctr Biotechnol Informat, Bethesda, MD 20892 USA
[3] Catholic Univ Amer, Washington, DC 20064 USA
[4] Scripps Res Inst, La Jolla, CA 92037 USA
[5] Albert Einstein Coll Med, Dept Physiol & Biophys, Bronx, NY 10461 USA
基金
美国国家卫生研究院;
关键词
ESCHERICHIA-COLI; PASSENGER PROTEINS; AUTOTRANSPORTER; SECRETION; ALIGNMENT; SIZE; PORE; INFORMATION; MECHANISM; RECEPTOR;
D O I
10.1016/j.str.2012.04.011
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
Intimins and invasins are virulence factors produced by pathogenic Gram-negative bacteria. They contain C-terminal extracellular passenger domains that are involved in adhesion to host cells and N-terminal 6 domains that are embedded in the outer membrane. Here, we identify the domain boundaries of an E. coli intimin beta domain and use this information to solve its structure and the beta domain structure of a Y. pseudotuberculosis invasin. Both beta domain structures crystallized as monomers and reveal that the previous range of residues assigned to the beta domain also includes a protease-resistant domain that is part of the passenger. Additionally, we identify 146 nonredundant representative members of the intimin/invasin family based on the boundaries of the highly conserved intimin and invasin beta domains. We then use this set, of sequences along with our structural data to find and map the evolutionarily constrained residues within the beta domain.
引用
收藏
页码:1233 / 1243
页数:11
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