1KN0

Crystal Structure of the human Rad52 protein

Summary for 1KN0

• Entry DOI: 10.2210/pdb1kn0/pdb
• Descriptor: Rad52 (2 entities in total)
• Functional Keywords: beta-beta-beta-alpha fold, dna-binding protein, ring protein, riken structural genomics/proteomics initiative, rsgi, structural genomics, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (Potential): P43351
• Total number of polymer chains: 11
• Total formula weight: 257746.61

Authors

Kagawa, W.,Kurumizaka, H.,Ishitani, R.,Fukai, S.,Nureki, O.,Shibata, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2001-12-18, release date: 2002-09-04, Last modification date: 2024-03-13)

Primary citation

Kagawa, W.,Kurumizaka, H.,Ishitani, R.,Fukai, S.,Nureki, O.,Shibata, T.,Yokoyama, S.
Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form.
Mol.Cell, 10:359-371, 2002

PubMed 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.

PubMed: 12191481
DOI: 10.1016/S1097-2765(02)00587-7

Experimental method

X-RAY DIFFRACTION (2.85 Å)