4E1S

X-ray crystal structure of the transmembrane beta-domain from intimin from EHEC strain O157:H7

Summary for 4E1S

• Entry DOI: 10.2210/pdb4e1s/pdb
• Related: 4E1T
• Descriptor: Intimin, CHLORIDE ION, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 entities in total)
• Functional Keywords: outer membrane beta barrel, adhesin, translocated intimin receptor, cell adhesion
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane; Single-pass membrane protein (By similarity): P43261
• Total number of polymer chains: 1
• Total formula weight: 32457.07

Authors

Fairman, J.W.,Dautin, N.,Wojtowicz, D.,Wei, L.,Noinaj, N.,Barnard, T.J.,Udho, E.,Finkelstein, A.,Przytycka, T.M.,Cherezov, V.,Buchanan, S.K. (deposition date: 2012-03-07, release date: 2012-06-13, Last modification date: 2024-02-28)

Primary citation

Fairman, J.W.,Dautin, N.,Wojtowicz, D.,Liu, W.,Noinaj, N.,Barnard, T.J.,Udho, E.,Przytycka, T.M.,Cherezov, V.,Buchanan, S.K.
Crystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosis.
Structure, 20:1233-1243, 2012

PubMed 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.

PubMed: 22658748
DOI: 10.1016/j.str.2012.04.011

Experimental method

X-RAY DIFFRACTION (1.855 Å)