The BioGRID | PUBLICATION VIEW

	Cell Biochem. Biophys. (2006); 46(1):17-26
Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1-7-A resolution-
Andi B, Cook PF, West AH
Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73019, USA-
Abstract: The three-dimensional structure of the saccharopine reductase enzyme from the budding yeast Saccharomyces cerevisiae was determined to 1-7-A resolution in the apo form by using molecular replacement- The enzyme monomer consists of three domains- domain I is a variant of the Rossmann fold, domain II folds into a alpha-beta structure containing a mixed seven-stranded beta-sheet as the central core, and domain III has an all-helical fold- Comparative fold alignment with the enzyme from Magnaporthe grisea suggests that domain I binds to NADPH, and domain II binds to saccharopine and is involved in dimer formation- Domain III is involved in closing the active site of the enzyme once substrates are bound- Structural comparison of the saccharopine reductase enzymes from S- cerevisiae and M- grisea indicates that domain II has the highest number of conserved residues, suggesting that it plays an important role in substrate binding and in spatially orienting domains I and III-
[PUBMED: 16943620]