1bi5
From Proteopedia
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|PDB= 1bi5 |SIZE=350|CAPTION= <scene name='initialview01'>1bi5</scene>, resolution 1.56Å | |PDB= 1bi5 |SIZE=350|CAPTION= <scene name='initialview01'>1bi5</scene>, resolution 1.56Å | ||
|SITE= <scene name='pdbsite=CYS:Catalytic+Site'>CYS</scene> | |SITE= <scene name='pdbsite=CYS:Catalytic+Site'>CYS</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bi5 OCA], [http://www.ebi.ac.uk/pdbsum/1bi5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bi5 RCSB]</span> | ||
}} | }} | ||
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[[Category: polyketide synthase]] | [[Category: polyketide synthase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:01:28 2008'' |
Revision as of 16:01, 30 March 2008
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| , resolution 1.56Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Naringenin-chalcone synthase, with EC number 2.3.1.74 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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