1kn0
From Proteopedia
Crystal Structure of the human Rad52 protein
Overview
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.
About this Structure
1KN0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form., Kagawa W, Kurumizaka H, Ishitani R, Fukai S, Nureki O, Shibata T, Yokoyama S, Mol Cell. 2002 Aug;10(2):359-71. PMID:12191481 Page seeded by OCA on Fri May 2 22:56:01 2008
Categories: Homo sapiens | Single protein | Fukai, S. | Ishitani, R. | Kagawa, W. | Kurumizaka, H. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shibata, T. | Yokoyama, S. | Beta-beta-beta-alpha fold | Dna-binding protein | Riken structural genomics/proteomics initiative | Ring protein | Rsgi | Structural genomic
