1kn0 | pdb_00001kn0
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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 Thu Feb 21 13:35:54 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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 genomics
