Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form

Mol Cell. 2002 Aug;10(2):359-71. doi: 10.1016/s1097-2765(02)00587-7.

Abstract

The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Crystallography, X-Ray
  • DNA / genetics
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Rad52 DNA Repair and Recombination Protein
  • Recombination, Genetic
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid*
  • Ultracentrifugation

Substances

  • DNA-Binding Proteins
  • RAD52 protein, human
  • Rad52 DNA Repair and Recombination Protein
  • DNA

Associated data

  • PDB/1KN0