2GAS

Crystal Structure of Isoflavone Reductase

Summary for 2GAS

• Entry DOI: 10.2210/pdb2gas/pdb
• Descriptor: isoflavone reductase (2 entities in total)
• Functional Keywords: nadph-dependent reductase, oxidoreductase
• Biological source: Medicago sativa
• Total number of polymer chains: 2
• Total formula weight: 68601.77

Authors

Wang, X.,He, X.,Lin, J.,Shao, H.,Chang, Z.,Dixon, R.A. (deposition date: 2006-03-09, release date: 2006-04-25, Last modification date: 2023-08-30)

Primary citation

Wang, X.,He, X.,Lin, J.,Shao, H.,Chang, Z.,Dixon, R.A.
Crystal Structure of Isoflavone Reductase from Alfalfa (Medicago sativa L.)
J.Mol.Biol., 358:1341-1352, 2006

PubMed Abstract: 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.

PubMed: 16600295
DOI: 10.1016/j.jmb.2006.03.022

Experimental method

X-RAY DIFFRACTION (1.6 Å)