1cml
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(New page: 200px<br /><applet load="1cml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cml, resolution 1.690Å" /> '''CHALCONE SYNTHASE F...)
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Revision as of 10:27, 20 November 2007
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CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH MALONYL-COA
Overview
Chalcone synthase (CHS) is pivotal for the biosynthesis of flavonoid, antimicrobial phytoalexins and anthocyanin pigments in plants. It produces, chalcone by condensing one p-coumaroyl- and three malonyl-coenzyme A, thioesters into a polyketide reaction intermediate that cyclizes. The, crystal structures of CHS alone and complexed with substrate and product, analogs reveal the active site architecture that defines the sequence and, chemistry of multiple decarboxylation and condensation reactions and, provides a molecular understanding of the cyclization reaction leading to, chalcone synthesis. The structure of CHS complexed with resveratrol also, suggests how stilbene synthase, a related enzyme, uses the same substrates, and an alternate cyclization pathway to form resveratrol. By using the, three-dimensional structure and the large database of CHS-like sequences, we can identify proteins likely to possess novel substrate and product, specificity. The structure elucidates the chemical basis of plant, polyketide biosynthesis and provides a framework for engineering CHS-like, enzymes to produce new products.
About this Structure
1CML is a Single protein structure of sequence from Medicago sativa with SO4, MLC and PIN as ligands. Active as Naringenin-chalcone synthase, with EC number 2.3.1.74 Full crystallographic information is available from OCA.
Reference
Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis., Ferrer JL, Jez JM, Bowman ME, Dixon RA, Noel JP, Nat Struct Biol. 1999 Aug;6(8):775-84. PMID:10426957
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