title: Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli.
abstract: Enteropathogenic Escherichia coli (EPEC) induce gross cytoskeletal rearrangement within epithelial cells, immediately beneath the attached bacterium. The C-terminal 280 amino acid residues of intimin (Int280; 30.1 kDa), a bacterial cell-adhesion molecule, mediate the intimate bacterial host-cell interaction. Recently, interest in this process has been stimulated by the discovery that the bacterial intimin receptor protein (Tir) is translocated into the host cell membrane, phosphorylated, and after binding intimin triggers the intimate attachment. Using multidimensional nuclear magnetic resonance (NMR) and combining perdeuteration with site-specific protonation of methyl groups, we have determined the global fold of Int280. This represents one of the largest, non-oligomeric protein structures to be determined by NMR that has not been previously resolved by X-ray crystallography. Int280 comprises three domains; two immunoglobulin-like domains and a C-type lectin-like module, which define a new family of bacterial adhesion molecules. These findings also imply that carbohydrate recognition may be important in intimin-mediated cell adhesion.
authors: Department of Biochemistry and Centre for Structural Biology, Imperial College of Science, Technology and Medicine, South Kensington, London, UK.
authors: G
authors: G
authors: Kelly
authors: S
authors: S
authors: Prasannan
authors: S
authors: S
authors: Daniell
authors: K
authors: K
authors: Fleming
authors: G
authors: G
authors: Frankel
authors: G
authors: G
authors: Dougan
authors: I
authors: I
authors: Connerton
authors: S
authors: S
authors: Matthews
mesh_terms: D018829:Adhesins, Bacterial; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion / Q000502:physiology*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000502:physiology; D002352:Carrier Proteins; D004926:Escherichia coli / Q000737:chemistry / Q000472:pathogenicity* / Q000502:physiology; D029968:Escherichia coli Proteins; D007136:Immunoglobulins / Q000737:chemistry; D037102:Lectins / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid
chemical_list: D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D007136:Immunoglobulins; D037102:Lectins; D010446:Peptide Fragments; C073819:eaeA protein, E coli