1e5u | pdb_00001e5u

NMR REPRESENTATIVE STRUCTURE OF INTIMIN-190 (INT190) FROM ENTEROPATHOGENIC E. COLI

spinqualitylabelsall models 1e5u, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1e5u is a 1 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entries and 1inm. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: EAE (Escherichia coli) Resources: FirstGlance, OCA, RCSB, PDBsum Function [EAE_ECO27] Necessary for the production of attaching and effacing lesions on tissue culture cells. Believed to mediate adherence. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Intimin is a bacterial adhesion molecule involved in intimate attachment of enteropathogenic and enterohaemorrhagic Escherichia coli to mammalian host cells. Intimin targets the translocated intimin receptor (Tir), which is exported by the bacteria and integrated into the host cell plasma membrane. In this study we localized the Tir-binding region of intimin to the C-terminal 190 amino acids (Int190). We have also determined the region's high-resolution solution structure, which comprises an immunoglobulin domain that is intimately coupled to a novel C-type lectin domain. This fragment, which is necessary and sufficient for Tir interaction, defines a new super domain in intimin that exhibits striking structural similarity to the integrin-binding domain of the Yersinia invasin and C-type lectin families. The extracellular portion of intimin comprises an articulated rod of immunoglobulin domains extending from the bacterium surface, conveying a highly accessible 'adhesive tip' to the target cell. The interpretation of NMR-titration and mutagenesis data has enabled us to identify, for the first time, the binding site for Tir, which is located at the extremity of the Int190 moiety. Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli.,Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, Bloomberg G, Dougan G, Frankel G, Matthews S EMBO J. 2000 Jun 1;19(11):2452-64. PMID:10835344 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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