1bi5
From Proteopedia
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| - | [[Image:1bi5.gif|left|200px]]<br /><applet load="1bi5" size=" | + | [[Image:1bi5.gif|left|200px]]<br /><applet load="1bi5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bi5, resolution 1.56Å" /> | caption="1bi5, resolution 1.56Å" /> | ||
'''CHALCONE SYNTHASE FROM ALFALFA'''<br /> | '''CHALCONE SYNTHASE FROM ALFALFA'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Active as [http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] Known structural/functional Site: <scene name='pdbsite=CYS:Catalytic Site'>CYS</scene>. Full crystallographic information is available from [http:// | + | 1BI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Active as [http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] Known structural/functional Site: <scene name='pdbsite=CYS:Catalytic+Site'>CYS</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BI5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: polyketide synthase]] | [[Category: polyketide synthase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:32:59 2008'' |
Revision as of 07:32, 3 February 2008
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CHALCONE SYNTHASE FROM ALFALFA
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
1BI5 is a Single protein structure of sequence from Medicago sativa. Active as Naringenin-chalcone synthase, with EC number 2.3.1.74 Known structural/functional Site: . 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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