2g1k: Difference between revisions

Revision as of 14:02, 29 July 2008

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File:2g1k.png

Template:STRUCTURE 2g1k

Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimate at 1.75 angstrom resolutionCrystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimate at 1.75 angstrom resolution

Template:ABSTRACT PUBMED 16834327

About this StructureAbout this Structure

2G1K is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimic acid and an ATP analogue., Gan J, Gu Y, Li Y, Yan H, Ji X, Biochemistry. 2006 Jul 18;45(28):8539-45. PMID:16834327

Page seeded by OCA on Tue Jul 29 14:02:52 2008

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OCA

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-'''Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimate at 1.75 angstrom resolution'''
+===Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimate at 1.75 angstrom resolution===
-==Overview==
+<!--
-Shikimate kinase (SK) and other enzymes in the shikimate pathway are potential targets for developing nontoxic antimicrobial agents, herbicides, and antiparasite drugs, because the pathway is essential in microorganisms, plants, and parasites but absent from mammals. SK catalyzes the reaction of phosphoryl transfer from ATP to shikimic acid (SA). Since 2002, a total of 11 SK structures have been reported, but none contains either the two substrate (SA and ATP) or the two product (SA-phosphate and ADP) molecules. Here, we present three crystal structures of SK from Mycobacterium tuberculosis (MtSK), including apo-MtSK, a binary complex MtSK x SA, and the ternary complex of MtSK with SA and an ATP analogue, AMPPCP. The structures of apo-MtSK and MtSK x AMPPCP x SA make it possible to elucidate the conformational changes of MtSK upon the binding of both substrates; the structure of MtSK x AMPPCP x SA reveals interactions between the protein and gamma-phosphate which indicate dynamic roles of catalytic residues Lys15 and Arg117.
+The line below this paragraph, {{ABSTRACT_PUBMED_16834327}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16834327 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16834327}}
 ==About this Structure==
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 [[Category: Shikimate pathway]]
 [[Category: Ternary complex]]
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