2fp1: Difference between revisions

Revision as of 19:01, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fp1.png

Template:STRUCTURE 2fp1

Secreted Chorismate Mutase from Mycobacterium tuberculosisSecreted Chorismate Mutase from Mycobacterium tuberculosis

Template:ABSTRACT PUBMED 16499927

About this StructureAbout this Structure

2FP1 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-'''Secreted Chorismate Mutase from Mycobacterium tuberculosis'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16499927}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Sasso, S.]]
 [[Category: Alpha-helical]]
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