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- W1994587584 abstract "Adenylosuccinate synthetase from Saccharomyces cerevisiae was investigated in order to find a structural explanation for its ability to bind specifically to single-stranded ARS elements (autonomously replicating sequences). Using the E. coli enzyme as template, a model for the structure of adenylosuccinate synthetase from S. cerevisiae was generated and subsequently refined by molecular dynamics techniques. The resulting three-dimensional structure offers an explanation for the DNA binding activity of the yeast enzyme by revealing a distinct basic region that is not present in the homologous enzymes from other organisms. The model is also in good agreement with biochemical data available for a mutant protein in which Glycine 252 is replaced by Aspartate. On the basis of the model a significant structural distortion near the catalytic center was predicted for this mutant, corresponding well to the enzymatic inactivity observed. The mutant enzyme shows larger structural fluctuations than the wild-type protein according to the results of two independent molecular dynamics simulations." @default.
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- W1994587584 date "1997-06-01" @default.
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- W1994587584 title "Homology Modeling of Adenylosuccinate Synthetase fromSaccharomyces CerevisiaeReveals a Possible Binding Region for Single-Stranded ARS Sequences" @default.
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- W1994587584 doi "https://doi.org/10.1080/07391102.1997.10508170" @default.
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