Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis

James W. Fairman, Nathalie Dautin, Damian Wojtowicz, Wei Liu, Nicholas Noinaj, Travis J. Barnard, Eshwar Udho, Teresa M. Przytycka, Vadim Cherezov, Susan K. Buchanan

Research output: Contribution to journalArticle

61 Scopus citations

Abstract

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 β domains that are embedded in the outer membrane. Here, we identify the domain boundaries of an E. coli intimin β domain and use this information to solve its structure and the β domain structure of a Y. pseudotuberculosis invasin. Both β domain structures crystallized as monomers and reveal that the previous range of residues assigned to the β 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 β domains. We then use this set of sequences along with our structural data to find and map the evolutionarily constrained residues within the β domain.

Original languageEnglish (US)
Pages (from-to)1233-1243
Number of pages11
JournalStructure
Volume20
Issue number7
DOIs
StatePublished - Jul 3 2012
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Fairman, J. W., Dautin, N., Wojtowicz, D., Liu, W., Noinaj, N., Barnard, T. J., Udho, E., Przytycka, T. M., Cherezov, V., & Buchanan, S. K. (2012). Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis. Structure, 20(7), 1233-1243. https://doi.org/10.1016/j.str.2012.04.011