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B6db references: 9655342

type Journal Article
authors Jeffery, C. J.; Barry, T.; Doonan, S.; Petsko, G. A.; Ringe, D.
title Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase
journal Protein Sci
sel selected
ui 9655342
year (1998)
volume 7
number 6
pages 1380-7
keywords Animal
abstract The crystal structure of Saccharomyces cerevisiae cytoplasmic aspartate aminotransferase (EC has been determined to 2.05 A resolution in the presence of the cofactor pyridoxal-5'-phosphate and the competitive inhibitor maleate. The structure was solved by the method of molecular replacement. The final value of the crystallographic R- factor after refinement was 23.1% with good geometry of the final model. The yeast cytoplasmic enzyme is a homodimer with two identical active sites containing residues from each subunit. It is found in the "closed" conformation with a bound maleate inhibitor in each active site. It shares the same three-dimensional fold and active site residues as the aspartate aminotransferases from Escherichia coli, chicken cytoplasm, and chicken mitochondria, although it shares less than 50% sequence identity with any of them. The availability of four similar enzyme structures from distant regions of the evolutionary tree provides a measure of tolerated changes that can arise during millions of years of evolution.
last changed 2010/11/09 16:02

B6db references