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Related Experiment Videos

Structural symmetry and protein function.

D S Goodsell1, A J Olson

  • 1Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037, USA. goodsell@scripps.edu, olson@scripps.edu

Annual Review of Biophysics and Biomolecular Structure
|August 15, 2000
PubMed
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Protein evolution favors symmetrical structures for stability and efficient assembly. While symmetry is common, various forms of asymmetry exist, driven by specific cellular functions and interactions.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • Most cellular proteins exist as symmetrical oligomeric complexes.
  • Oligomerization offers advantages in protein stability, function, and genetic efficiency.
  • Symmetry is a prevalent feature in protein complex evolution.

Purpose of the Study:

  • To explore the evolutionary drivers and diverse forms of symmetry in protein complexes.
  • To understand how functional, genetic, and physicochemical factors influence protein quaternary structure.
  • To investigate the prevalence and mechanisms of asymmetry in protein assemblies.

Main Methods:

  • Analysis of protein structures and evolutionary principles.
  • Review of literature on protein complex formation and symmetry.

Related Experiment Videos

  • Examination of various symmetry types and their functional implications.

    • Main Results:

    • Symmetrical oligomers are selected for morphological and cooperative functions, enhanced stability, and efficient synthesis.
    • Functional constraints like DNA/membrane interactions or directional motion can limit or break symmetry.
    • Various forms of asymmetry, including local, reciprocating, and global, are observed, with dimers often favored evolutionarily.

    Conclusions:

    • Protein complex evolution balances the benefits of symmetry with functional demands, leading to diverse structural solutions.
    • While symmetry offers advantages, evolutionary pressures can lead to various forms of asymmetry to meet specific cellular needs.
    • All crystallographic point groups are represented in protein structures, highlighting the adaptability of symmetry in evolution.