Analysis of the low-frequency normal modes of the R state of aspartate transcarbamylase and a comparison with the T state modes.

@article{Thomas1996AnalysisOT,
  title={Analysis of the low-frequency normal modes of the R state of aspartate transcarbamylase and a comparison with the T state modes.},
  author={Aline Thomas and Martin J. Field and David P{\'e}rahia},
  journal={Journal of molecular biology},
  year={1996},
  volume={261 3},
  pages={490-506}
}
Aspartate transcarbamylase (ATCase) is a classic example of an allosteric enzyme. It catalyzes the conversion of aspartate to carbamyl aspartate, which is the first substrate in the biosynthesis of pyrimidines. Although ATCase is well characterized, both structurally and biochemically, little is known at the atomic level about the large amplitude motions that govern its T-->R quaternary transition. We present the results of calculations of the very-low-frequency normal modes of the CTP-ligated… CONTINUE READING

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