2gpt
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(New page: 200px<br /><applet load="2gpt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gpt, resolution 1.95Å" /> '''Crystal structure of...)
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Revision as of 09:12, 21 November 2007
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Crystal structure of Arabidopsis Dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate
Overview
The bifunctional enzyme dehydroquinate dehydratase-shikimate dehydrogenase, (DHQ-SDH) catalyzes the dehydration of dehydroquinate to dehydroshikimate, and the reduction of dehydroshikimate to shikimate in the shikimate, pathway. We report the first crystal structure of Arabidopsis DHQ-SDH with, shikimate bound at the SDH site and tartrate at the DHQ site. The, interactions observed in the DHQ-tartrate complex reveal a conserved mode, for substrate binding between the plant and microbial DHQ dehydratase, family of enzymes. The SDH-shikimate complex provides the first direct, evidence of the role of active site residues in the catalytic mechanism., Site-directed mutagenesis and mechanistic analysis revealed that Asp 423, and Lys 385 are key catalytic groups and Ser 336 is a key binding group., The arrangement of the two functional domains reveals that the control of, metabolic flux through the shikimate pathway is achieved by increasing the, effective concentration of dehydroshikimate through the proximity of the, two sites.
About this Structure
2GPT is a Single protein structure of sequence from Arabidopsis thaliana with SO4, TLA and SKM as ligands. Full crystallographic information is available from OCA.
Reference
Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway., Singh SA, Christendat D, Biochemistry. 2006 Jun 27;45(25):7787-96. PMID:16784230
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