4e1t
X-ray crystal structure of the transmembrane beta-domain from invasin from Yersinia pseudotuberculosisX-ray crystal structure of the transmembrane beta-domain from invasin from Yersinia pseudotuberculosis
Structural highlights
Function[INVA_YERPS] Invasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins. Publication Abstract from PubMedIntimins 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 beta 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. Crystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosis.,Fairman JW, Dautin N, Wojtowicz D, Liu W, Noinaj N, Barnard TJ, Udho E, Przytycka TM, Cherezov V, Buchanan SK Structure. 2012 May 31. PMID:22658748[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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