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Related Experiment Videos

Modelling allosteric processes in E coli aspartate transcarbamylase.

J Cherfils1, P Vachette, J Janin

  • 1Laboratoire de Biologie Physicochimique (UA 1131 CNRS), Université Paris-Sud, Orsay, France.

Biochimie
|August 1, 1990
PubMed
Summary

Aspartate transcarbamylase allosteric regulation was studied using genetic and structural methods. Key interfaces were identified, and mutations affecting them reduced enzyme cooperativity and allosteric control.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enymology

Background:

  • Aspartate transcarbamylase (ATCase) is a key enzyme in pyrimidine biosynthesis.
  • Its allosteric properties are crucial for metabolic regulation.
  • Previous X-ray structures revealed T and R states of ATCase.

Purpose of the Study:

  • To investigate the allosteric properties of aspartate transcarbamylase from E. coli.
  • To identify subunit interfaces critical for the allosteric mechanism.
  • To model mutations and understand their impact on enzyme function.

Main Methods:

  • Genetic studies
  • Biochemical assays
  • X-ray crystallography
  • Molecular mechanics simulations

Related Experiment Videos

  • Site-directed mutagenesis

    • Main Results:

    • Identified c1c4 and c1r4 interfaces crucial for allosteric regulation.
    • Modeled mutations pAR5 and Tyr240Phe, showing reduced cooperativity and/or allosteric regulation.
    • Molecular mechanics simulations provided structural insights into mutation effects.
    • Modeled substrate binding in the T state, noting weaker aspartate binding compared to the R state.

    Conclusions:

    • Subunit interfaces play a major role in ATCase allosteric mechanism.
    • Specific mutations at these interfaces disrupt enzyme cooperativity and regulation.
    • Structural modeling and simulations offer testable hypotheses for enzyme function.