2axq

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Revision as of 06:19, 21 November 2007

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spinqualitylabelsall models 2axq, resolution 1.700Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae

Overview

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.

About this Structure

2AXQ is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 as ligand. Active as Saccharopine dehydrogenase (NADP(+), L-glutamate-forming), with EC number 1.5.1.10 Full crystallographic information is available from OCA.

Reference

Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-A resolution., Andi B, Cook PF, West AH, Cell Biochem Biophys. 2006;46(1):17-26. PMID:16943620

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