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Related Experiment Videos

Recurring structural motifs in proteins with different functions.

C A Orengo1, T P Flores, D T Jones

  • 1Biomolecular Structure and Modelling Unit, Department of Biochemistry Molecular Biology, University College, Gower Street, London WC1E 6BT, UK.

Current Biology : CB
|March 1, 1993
PubMed
Summary

Protein structural folds can be similar even without shared ancestry or function. This study identified new examples of convergent evolution in protein structures, highlighting criteria for favorable fold generation.

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Area of Science:

  • Structural biology
  • Bioinformatics
  • Protein folding

Background:

  • Proteins diverging from a common ancestor often retain structural and sequence similarity.
  • However, proteins with different functions can converge to similar structures despite low sequence identity.

Purpose of the Study:

  • To identify novel instances of proteins with similar structures but no apparent sequence or functional similarity.
  • To investigate the evolutionary and biophysical principles underlying protein fold conservation.

Main Methods:

  • Comprehensive comparison of the protein structure database using sequence and structure alignment algorithms.
  • Analysis of identified structural similarities within small proteins and as motifs in larger proteins.

Main Results:

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  • Six new examples of structurally related protein folds lacking sequence or functional similarity were discovered.
  • Identified families include crambin-like and ferredoxin II-like folds.
  • Structural similarities were found in small proteins or as core motifs in larger ones.

Conclusions:

  • Similar structures with low sequence similarity suggest independent evolutionary origins (convergent evolution).
  • These findings offer insights into the stereochemical and physical factors governing the formation of stable protein folds.
  • The study underscores that structural similarity does not always imply common ancestry or shared function.