The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A

J Mol Biol. 2003 Jul 11;330(3):503-11. doi: 10.1016/s0022-2836(03)00473-x.

Abstract

MacroH2A is an unusual histone H2A variant that has an extensive C-terminal tail that comprises approximately two thirds of the protein. The C-terminal non-histone domain of macroH2A is also found in a number of other proteins and has been termed the macro domain. Here we report the crystal structure to 1.7A of AF1521, a protein consisting of a stand-alone macro domain from Archaeoglobus fulgidus. The structure has a mixed alpha/beta fold that closely resembles the N-terminal DNA binding domain of the Escherichia coli leucine aminopeptidase PepA. The structure also shows some similarity to members of the P-loop family of nucleotide hydrolases.

MeSH terms

  • Amino Acid Sequence
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / metabolism*
  • Archaeoglobus fulgidus / chemistry*
  • Bacterial Proteins / chemistry
  • Binding Sites
  • Crystallography, X-Ray
  • DNA / metabolism
  • Dosage Compensation, Genetic
  • Histones / chemistry*
  • Hydrolases / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary
  • RNA / metabolism
  • Sequence Homology, Amino Acid
  • Structural Homology, Protein

Substances

  • Archaeal Proteins
  • Bacterial Proteins
  • Histones
  • macroH2A histone
  • pseudomonas exoprotein A protein, Pseudomonas aeruginosa
  • RNA
  • DNA
  • Hydrolases