1gu1: Difference between revisions
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[[Category: type ii dehydroquinase]] | [[Category: type ii dehydroquinase]] | ||
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Revision as of 16:14, 30 October 2007
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CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR COMPLEXED WITH 2,3-ANYDRO-QUINIC ACID
OverviewOverview
The structure of the type II DHQase from Streptomyces coelicolor has been, solved and refined to high resolution in complexes with a number of, ligands, including dehydroshikimate and a rationally designed transition, state analogue, 2,3-anhydro-quinic acid. These structures define the, active site of the enzyme and the role of key amino acid residues and, provide snap shots of the catalytic cycle. The resolution of the flexible, lid domain (residues 21-31) shows that the invariant residues Arg23 and, Tyr28 close over the active site cleft. The tyrosine acts as the base in, the initial proton abstraction, and evidence is provided that the reaction, proceeds via an enol intermediate. The active site of the structure of, DHQase in complex with the transition state analog also includes ... [(full description)]
About this StructureAbout this Structure
1GU1 is a [Single protein] structure of sequence from [Streptomyces coelicolor] with FA1, TLA, TRS and GOL as [ligands]. Active as [3-dehydroquinate dehydratase], with EC number [4.2.1.10]. Structure known Active Site: FAA. Full crystallographic information is available from [OCA].
ReferenceReference
The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor., Roszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ, Structure. 2002 Apr;10(4):493-503. PMID:11937054
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