1b22: Difference between revisions
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'''RAD51 (N-TERMINAL DOMAIN)''' | '''RAD51 (N-TERMINAL DOMAIN)''' | ||
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[[Category: Shibata, T.]] | [[Category: Shibata, T.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: | [[Category: Dna binding]] | ||
[[Category: | [[Category: Riken structural genomics/proteomics initiative]] | ||
[[Category: | [[Category: Rsgi]] | ||
[[Category: | [[Category: Structural genomic]] | ||
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Revision as of 07:57, 2 May 2008
RAD51 (N-TERMINAL DOMAIN)
Overview
Human Rad51 protein (HsRad51) is a homolog of Escherichia coli RecA protein, and functions in DNA repair and recombination. In higher eukaryotes, Rad51 protein is essential for cell viability. The N-terminal region of HsRad51 is highly conserved among eukaryotic Rad51 proteins but is absent from RecA, suggesting a Rad51-specific function for this region. Here, we have determined the structure of the N-terminal part of HsRad51 by NMR spectroscopy. The N-terminal region forms a compact domain consisting of five short helices, which shares structural similarity with a domain of endonuclease III, a DNA repair enzyme of E. coli. NMR experiments did not support the involvement of the N-terminal domain in HsRad51-HsBrca2 interaction or the self-association of HsRad51 as proposed by previous studies. However, NMR tiration experiments demonstrated a physical interaction of the domain with DNA, and allowed mapping of the DNA binding surface. Mutation analysis showed that the DNA binding surface is essential for double-stranded and single-stranded DNA binding of HsRad51. Our results suggest the presence of a DNA binding site on the outside surface of the HsRad51 filament and provide a possible explanation for the regulation of DNA binding by phosphorylation within the N-terminal domain.
About this Structure
1B22 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR., Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T, J Mol Biol. 1999 Jul 9;290(2):495-504. PMID:10390347 Page seeded by OCA on Fri May 2 10:57:57 2008
