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Related Experiment Videos

Quantification of tertiary structural conservation despite primary sequence drift in the globin fold

H E Aronson1, W E Royer, W A Hendrickson

  • 1Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.

Protein Science : a Publication of the Protein Society
|October 1, 1994
PubMed
Summary

Protein structural inertia is demonstrated by comparing diverse hemoglobin subunits. Despite low sequence similarity, their core structures remain remarkably conserved, highlighting evolutionary resilience.

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Structural Biology

Background:

  • The globin protein family was the first observed to maintain conserved tertiary structure despite significant divergence in primary amino acid sequences.
  • This principle of structural inertia is now recognized across many protein families, indicating a fundamental aspect of molecular evolution.

Purpose of the Study:

  • To systematically compare the sequences and structures of six diverse hemoglobin subunits from plants, clams, and humans.
  • To investigate the relationship between sequence similarity and structural conservation in the globin family.

Main Methods:

  • Comparative analysis of amino acid sequences and 3D structures of six representative hemoglobin subunits.
  • Focus on a conserved 97-residue helical core common to all analyzed structures.

Related Experiment Videos

  • Calculation of pairwise sequence identities and root-mean-square deviation (RMSD) of alpha-carbon positions.

    • Main Results:

    • Amino acid sequence identities ranged from 12.4% to 42.3%.
    • Maximal RMS deviation in alpha-carbon positions was 3.02 Å, indicating high structural similarity.
    • A significant negative correlation (r = -0.71) was observed between sequence similarity and structural deviation, weakening at <20% sequence identity (r = -0.38).
    • Substantial variability exists outside the helical core, with differing functional characteristics among globins.

    Conclusions:

    • The core structures of diverse globins are remarkably preserved despite significant sequence dissimilarities and functional variations.
    • The study emphasizes the weak direct link between specific amino acid sequences and the resulting tertiary protein fold.
    • Structural inertia plays a crucial role in protein evolution, allowing functional proteins to evolve from divergent sequences.