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Related Experiment Videos

GCN5-related N-acetyltransferases: a structural overview.

F Dyda1, D C Klein, A B Hickman

  • 1Laboratory of Molecular Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA. dyda@ulti.niddk.nih.gov

Annual Review of Biophysics and Biomolecular Structure
|August 15, 2000
PubMed
Summary

This review explores the structures of GCN5-related N-acetyltransferases (GNATs), a superfamily of enzymes. Despite varied functions, GNATs share similar structures and acetyl-CoA binding, suggesting a conserved catalytic mechanism.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Acetyltransferases are enzymes that transfer acetyl groups, utilizing acetyl coenzyme A (acetyl-CoA) as a common donor.
  • These enzymes display high specificity for their diverse acetyl acceptors, including small molecules and proteins.
  • Sequence analysis reveals that acetyltransferases can be classified into several superfamilies.

Purpose of the Study:

  • To review the three-dimensional structures of enzymes within the GCN5-related N-acetyltransferase (GNAT) superfamily.
  • To highlight the structural similarities and conserved features among diverse GNAT members.
  • To explore the implications of these structural similarities for understanding their catalytic mechanisms.

Main Methods:

  • Structural analysis of GNAT superfamily members.

Related Experiment Videos

  • Comparison of protein topology and substrate binding modes.
  • Literature review of existing structural and functional data.

    • Main Results:

    • Members of the GNAT superfamily exhibit remarkable similarity in their overall protein topology.
    • A conserved mode of binding for the acetyl donor, acetyl-CoA, is observed across GNATs.
    • Despite diverse substrate specificities, structural conservation suggests a common evolutionary origin and catalytic strategy.

    Conclusions:

    • The GNAT superfamily, including histone acetyltransferases, shares fundamental structural characteristics.
    • The conserved structural features and acetyl-CoA binding mode point to a conserved catalytic mechanism within the GNAT superfamily.
    • Understanding these structural similarities provides insights into the functional diversity and evolution of N-acetyltransferases.