1f02 | pdb_00001f02

CRYSTAL STRUCTURE OF C-TERMINAL 282-RESIDUE FRAGMENT OF INTIMIN IN COMPLEX WITH TRANSLOCATED INTIMIN RECEPTOR (TIR) INTIMIN-BINDING DOMAIN

spinqualitylabelsall models 1f02, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1f02 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1f00, 1inm, 1cwv Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 and its translocated intimin receptor (Tir) are bacterial proteins that mediate adhesion between mammalian cells and attaching and effacing (A/E) pathogens. Enteropathogenic Escherichia coli (EPEC) causes significant paediatric morbidity and mortality world-wide. A related A/E pathogen, enterohaemorrhagic E. coli (EHEC; O157:H7) is one of the most important food-borne pathogens in North America, Europe and Japan. A unique and essential feature of A/E bacterial pathogens is the formation of actin-rich pedestals beneath the intimately adherent bacteria and localized destruction of the intestinal brush border. The bacterial outer membrane adhesin, intimin, is necessary for the production of the A/E lesion and diarrhoea. The A/E bacteria translocate their own receptor for intimin, Tir, into the membrane of mammalian cells using the type III secretion system. The translocated Tir triggers additional host signalling events and actin nucleation, which are essential for lesion formation. Here we describe the the crystal structures of an EPEC intimin carboxy-terminal fragment alone and in complex with the EPEC Tir intimin-binding domain, giving insight into the molecular mechanisms of adhesion of A/E pathogens. Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex.,Luo Y, Frey EA, Pfuetzner RA, Creagh AL, Knoechel DG, Haynes CA, Finlay BB, Strynadka NC Nature. 2000 Jun 29;405(6790):1073-7. PMID:10890451 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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