2fp2
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(New page: 200px<br /><applet load="2fp2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fp2, resolution 1.64Å" /> '''Secreted Chorismate ...)
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Revision as of 17:41, 29 January 2008
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Secreted Chorismate Mutase from Mycobacterium tuberculosis
Overview
The presence of exported chorismate mutases produced by certain organisms, such as Mycobacterium tuberculosis has been shown to correlate with their, pathogenicity. As such, these proteins comprise a new group of promising, selective drug targets. Here, we report the high-resolution crystal, structure of the secreted dimeric chorismate mutase from M. tuberculosis, (*MtCM; encoded by Rv1885c), which represents the first 3D-structure of a, member of this chorismate mutase family, termed the AroQ(gamma) subclass., Structures are presented both for the unliganded enzyme and for a complex, with a transition state analog. The protomer fold resembles the, structurally characterized (dimeric) Escherichia coli chorismate mutase, domain, but exhibits a new topology, with helix H4 of *MtCM carrying the, catalytic site residue missing in the shortened helix H1. Furthermore, the, structure of each *MtCM protomer is significantly more compact and only, harbors one active site pocket, which is formed entirely by one, polypeptide chain. Apart from the structural model, we present evidence as, to how the substrate may enter the active site.
About this Structure
2FP2 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as Chorismate mutase, with EC number 5.4.99.5 Full crystallographic information is available from OCA.
Reference
1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed., Okvist M, Dey R, Sasso S, Grahn E, Kast P, Krengel U, J Mol Biol. 2006 Apr 14;357(5):1483-99. Epub 2006 Feb 6. PMID:16499927
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