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The actin fold

W Kabsch1, K C Holmes

  • 1Max-Planck-Institut für medizinische Forschung, Abteilung Biophysik, Heidelberg, Germany.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|February 1, 1995
PubMed
Summary
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Structural analysis reveals actin and Hsc70 share a common fold despite different sequences. This suggests evolutionary gene duplication and a conserved nucleotide-binding site across diverse ATPases and kinases.

Area of Science:

  • Structural biology
  • Protein biochemistry
  • Evolutionary biology

Background:

  • Actin and heat-shock cognate protein 70 (Hsc70) are crucial proteins with distinct functions.
  • Previous studies indicated limited sequence homology between actin and Hsc70.

Purpose of the Study:

  • To investigate the structural relationship between actin and the NH2-terminal domain of Hsc70.
  • To identify conserved structural motifs and evolutionary origins.

Main Methods:

  • X-ray structure analysis of actin and Hsc70 NH2-terminal domain.
  • Comparative structural alignment and sequence fingerprinting.
  • Database searches for homologous proteins.

Main Results:

Related Experiment Videos

  • Actin and Hsc70 share extensive structural similarity, including a common core architecture and nucleotide-binding site.
  • Both proteins exhibit a conserved alpha/beta fold with two domains and a nucleotide-binding pocket, resembling hexokinase.
  • The structural similarity suggests evolution by gene duplication, with conserved nucleotide-binding pockets and variable functional regions.

    • Conclusions:

    • A conserved protein fold and nucleotide-binding site exist between actin and Hsc70, despite low sequence similarity.
    • This fold is likely conserved across various ATPases, kinases (e.g., glycerol kinase), and prokaryotic proteins (e.g., FtsA, MreB).
    • Functional diversity arises from variations in loop regions and inserted domains surrounding the conserved core structure.