1E5U
NMR Representative Structure of Intimin-190 (Int190) from Enteropathogenic E. coli
Replaces: 1E1BReplaces: 1INMSummary for 1E5U
| Entry DOI | 10.2210/pdb1e5u/pdb |
| Descriptor | INTIMIN (1 entity in total) |
| Functional Keywords | intimin, escherichia coli, cell adhesion, outer membrane protein, nmr spectroscopy |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cell outer membrane; Single-pass membrane protein: P19809 |
| Total number of polymer chains | 1 |
| Total formula weight | 20074.33 |
| Authors | Prasannan, S.,Matthews, S.J.,Batchelor, M.,Daniell, S.,Reece, S.,Frankel, G.,Dougan, G.,Connerton, I.,Bloomberg, G. (deposition date: 2000-08-02, release date: 2000-08-16, Last modification date: 2024-10-16) |
| Primary citation | Batchelor, M.,Prasannan, S.,Daniell, S.,Reece, S.,Connerton, I.,Bloomberg, G.,Dougan, G.,Frankel, G.,Matthews, S.J. Structural Basis for Recognition of the Translocated Intimin Receptor (Tir) by Intimin from Enteropathogenic E. Coli Embo J., 19:2452-, 2000 Cited by PubMed Abstract: 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. PubMed: 10835344DOI: 10.1093/EMBOJ/19.11.2452 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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