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Protein structures sustain evolutionary drift

B Rost1

  • 1EMBL, Heidelberg, Germany. rost@embl-heidelberg.de

Folding & Design
|January 1, 1997
PubMed
Summary
This summary is machine-generated.

Protein structures are surprisingly stable despite sequence changes, with only a small percentage of

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Area of Science:

  • Structural biology
  • Protein bioinformatics
  • Evolutionary biology

Background:

  • Proteins fold into unique 3D structures, but different sequences can yield similar structures.
  • Understanding protein structure stability against sequence variations is crucial.
  • Identifying essential 'anchor' residues for structure and function is a key question.

Purpose of the Study:

  • To determine the stability of protein structures concerning sequence changes.
  • To quantify the percentage of 'anchor' residues critical for protein structure and function.
  • To analyze evolutionary pathways leading to structurally similar proteins.

Main Methods:

  • Analysis of large datasets of structurally homologous protein pairs.
  • Comparison of sequence identities between proteins with similar 3D structures.

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  • Statistical analysis of residue conservation and evolutionary divergence.

    • Main Results:

    • Structurally homologous proteins often exhibit low sequence identity (8-9%), similar to random sequences.
    • On average, only 3-4% of residues are identified as 'anchor' residues.
    • Evolutionary equilibrium for most structures appears to be reached within four billion years.
    • Distinguishing between convergent and divergent evolution is challenging due to similar mean sequence identities.

    Conclusions:

    • Protein structures demonstrate remarkable stability against significant sequence variation.
    • A small fraction of 'anchor' residues is sufficient to maintain structural integrity and function.
    • Low sequence identity does not necessarily imply convergent evolution; evolutionary equilibrium is a significant factor.