1r88
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(New page: 200px<br /><applet load="1r88" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r88, resolution 1.71Å" /> '''The crystal structur...)
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Revision as of 23:13, 20 November 2007
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The crystal structure of Mycobacterium tuberculosis MPT51 (FbpC1)
Overview
Mycobacterium tuberculosis, the causative agent of tuberculosis, is known, to secrete a number of highly immunogenic proteins that are thought to, confer pathogenicity, in part, by mediating binding to host tissues. Among, these secreted proteins are the trimeric antigen 85 (Ag85) complex and the, related MPT51 protein, also known as FbpC1. While the physiological, function of Ag85, a mycolyltransferase required for the biosynthesis of, the cell wall component alpha,alpha'-trehalose dimycolate (or cord, factor), has been identified recently, the function of the closely related, MPT51 (approximately 40% identity with the Ag85 components) remains to be, established. The crystal structure of M.tuberculosis MPT51, determined to, 1.7 A resolution, shows that MPT51, like the Ag85 components Ag85B and, Ag85C2, folds as an alpha/beta hydrolase, but it does not contain any of, the catalytic elements required for mycolyltransferase activity. Moreover, the absence of a recognizable alpha,alpha'-trehalose monomycolate-binding, site and the failure to detect an active site suggest that the function of, MPT51 is of a non-enzymatic nature and that MPT51 may in fact represent a, new family of non-catalytic alpha/beta hydrolases. Previous experimental, evidence and the structural similarity to some integrins and, carbohydrate-binding proteins led to the hypothesis that MPT51 might have, a role in host tissue attachment, whereby ligands may include the serum, protein fibronectin and small sugars.
About this Structure
1R88 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
The structure of Mycobacterium tuberculosis MPT51 (FbpC1) defines a new family of non-catalytic alpha/beta hydrolases., Wilson RA, Maughan WN, Kremer L, Besra GS, Futterer K, J Mol Biol. 2004 Jan 9;335(2):519-30. PMID:14672660
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