1e5u
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(New page: 200px<br /><applet load="1e5u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5u" /> '''NMR REPRESENTATIVE STRUCTURE OF INTIMIN-190 ...)
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Revision as of 11:40, 20 November 2007
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NMR REPRESENTATIVE STRUCTURE OF INTIMIN-190 (INT190) FROM ENTEROPATHOGENIC E. COLI
Overview
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.
About this Structure
1E5U is a Single protein structure of sequence from Escherichia coli. This structure superseeds the now removed PDB entry 1E1B. Full crystallographic information is available from OCA.
Reference
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
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