1w9a
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(New page: 200px<br /><applet load="1w9a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w9a, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 21:27, 24 November 2007
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CRYSTAL STRUCTURE OF RV1155 FROM MYCOBACTERIUM TUBERCULOSIS
Overview
With the aim of elucidating the biological function of hypothetical, proteins unique amongst the Actynomyces sub-group of bacteria, we have, solved the crystal structure of the conserved hypothetical protein Rv1155, from Mycobacterium tuberculosis at 1.8 A resolution. Rv1155 is a homodimer, both in the crystal structure and in solution and folds into two separate, domains consisting of a six-stranded anti-parallel beta-barrel fold, flanked by two alpha-helices and a helix-turn-helix domain. Both domains, contribute to the formation of two deep clefts at the dimer interface. The, overall fold of Rv1155 strikingly resembles that of flavin, mononucleotide-binding protein and pyridoxamine 5'-phosphate oxydase, but, the architecture of the putative binding pocket is markedly different, consistent with the lack of color of Rv1155 and its inability to bind FMN., Rv1155 thus appears to belong to a group of proteins with stringent, conservation of the binding cleft, having evolved towards a new binding, function.
About this Structure
1W9A is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis., Canaan S, Sulzenbacher G, Roig-Zamboni V, Scappuccini-Calvo L, Frassinetti F, Maurin D, Cambillau C, Bourne Y, FEBS Lett. 2005 Jan 3;579(1):215-21. PMID:15620716
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