1B22

RAD51 (N-TERMINAL DOMAIN)

Summary for 1B22

• Entry DOI: 10.2210/pdb1b22/pdb
• Descriptor: DNA REPAIR PROTEIN RAD51 (1 entity in total)
• Functional Keywords: dna binding, riken structural genomics/proteomics initiative, rsgi, structural genomics, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q06609
• Total number of polymer chains: 1
• Total formula weight: 12547.28

Authors

Aihara, H.,Ito, Y.,Kurumizaka, H.,Yokoyama, S.,Shibata, T.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 1998-12-04, release date: 1999-12-03, Last modification date: 2023-12-27)

Primary citation

Aihara, H.,Ito, Y.,Kurumizaka, H.,Yokoyama, S.,Shibata, T.
The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
J.Mol.Biol., 290:495-504, 1999

PubMed Abstract: 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.

PubMed: 10390347
DOI: 10.1006/jmbi.1999.2904

Experimental method

SOLUTION NMR