GCN5-related N-acetyltransferases: a structural overview

Annu Rev Biophys Biomol Struct. 2000;29:81-103. doi: 10.1146/annurev.biophys.29.1.81.

Abstract

Hundreds of acetyltransferases exist. All use a common acetyl donor--acetyl coenzyme A--and each exhibits remarkable specificity for acetyl acceptors, which include small molecules and proteins. Analysis of the primary sequences of these enzymes indicates that they can be sorted into several superfamilies. This review covers the three-dimensional structures of members of one of these superfamilies, now referred to in the literature as the GCN5-related N-acetyltransferases (GNAT), reflecting the importance of one functional category, the histone acetyltransferases. Despite the diversity of substrate specificities, members of the GNAT superfamily demonstrate remarkable similarity in protein topology and mode of acetyl coenzyme A binding, likely reflecting a conserved catalytic mechanism.

Publication types

  • Review

MeSH terms

  • Acetyl Coenzyme A / chemistry
  • Acetyl Coenzyme A / metabolism
  • Acetylation
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Catalysis
  • DNA-Binding Proteins*
  • Fungal Proteins / chemistry*
  • Histone Acetyltransferases
  • Histones / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Multigene Family
  • Protein Conformation
  • Protein Kinases / chemistry*
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid

Substances

  • DNA-Binding Proteins
  • Fungal Proteins
  • Histones
  • Saccharomyces cerevisiae Proteins
  • Acetyl Coenzyme A
  • GCN5 protein, S cerevisiae
  • Histone Acetyltransferases
  • Protein Kinases