2gas

From Proteopedia

Revision as of 08:57, 21 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

2gas, resolution 1.6Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Wed Nov 21 11:05:04 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools