2gas
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gas OCA], [http://www.ebi.ac.uk/pdbsum/2gas PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gas RCSB]</span> | ||
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[[Category: nadph-dependent reductase]] | [[Category: nadph-dependent reductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:14:13 2008'' |
Revision as of 00:14, 31 March 2008
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| , resolution 1.6Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Isoflavone Reductase
Overview
Isoflavonoids play important roles in plant defense and exhibit a range of mammalian health-promoting activities. Isoflavone reductase (IFR) specifically recognizes isoflavones and catalyzes a stereospecific NADPH-dependent reduction to (3R)-isoflavanone. The crystal structure of Medicago sativa IFR with deletion of residues 39-47 has been determined at 1.6A resolution. Structural analysis, molecular modeling and docking, and comparison with the structures of other NADPH-dependent enzymes, defined the putative binding sites for co-factor and substrate and potential key residues for enzyme activity and substrate specificity. Further mutagenesis has confirmed the role of Lys144 as a catalytic residue. This study provides a structural basis for understanding the enzymatic mechanism and substrate specificity of IFRs as well as the functions of IFR-like proteins.
About this Structure
2GAS is a Single protein structure of sequence from Medicago sativa. Full crystallographic information is available from OCA.
Reference
Crystal structure of isoflavone reductase from alfalfa (Medicago sativa L.)., Wang X, He X, Lin J, Shao H, Chang Z, Dixon RA, J Mol Biol. 2006 May 19;358(5):1341-52. Epub 2006 Mar 29. PMID:16600295
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