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Local frustration around enzyme active sites.

Maria I Freiberger1,2, A Brenda Guzovsky1, Peter G Wolynes3

  • 1Protein Physiology Laboratory, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires-Consejo Nacional de Investigaciones Científicas y Tecnológicas-Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales, C1428EGA Buenos Aires, Argentina.

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|February 16, 2019
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Summary

Protein enzyme active sites exhibit high energetic frustration, crucial for biological function. This local frustration pattern is evolutionarily conserved, even more so than the protein sequence itself.

Keywords:
bioinformaticscatalytic sitesevolutionlocal frustrationprotein enzymes

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • Proteins must balance conflicting biological goals for structure and function.
  • The principle of minimal frustration explains protein folding, but local violations create complex energy landscapes for biological activity.
  • Enzymes utilize these complex landscapes for their catalytic functions.

Purpose of the Study:

  • To investigate local energetic frustration patterns in protein enzyme catalytic sites.
  • To determine if these frustration patterns are conserved across enzyme families and evolution.
  • To understand the role of energetic frustration in enzyme function and evolution.

Main Methods:

  • Surveyed local energetic frustration patterns of all known protein enzyme structures.
  • Analyzed experimentally annotated catalytic residues.
  • Evaluated the conservation of energetic signatures in enzyme families.

Main Results:

  • Catalytic sites of enzymes are frequently highly frustrated, irrespective of protein characteristics.
  • A secondary shell of weakly frustrated interactions surrounds the catalytic site.
  • Local frustration signatures are more evolutionarily conserved than primary protein sequences.

Conclusions:

  • High local energetic frustration is a key feature of enzyme catalytic sites, essential for biological function.
  • Evolutionary conservation of these frustration patterns suggests their fundamental importance.
  • Energetic frustration patterns offer a conserved signature for understanding enzyme evolution and function.