2KZ3

Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Rad51D from 1 to 83

Summary for 2KZ3

• Entry DOI: 10.2210/pdb2kz3/pdb
• NMR Information: BMRB: 16996
• Descriptor: Putative uncharacterized protein RAD51L3 (1 entity in total)
• Functional Keywords: rad51d, homologous recombination, unknown function
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 9070.67

Authors

Choi, N.,Kim, Y. (deposition date: 2010-06-11, release date: 2011-01-05, Last modification date: 2024-05-15)

Primary citation

Kim, Y.M.,Choi, B.S.
Structural and functional characterization of the N-terminal domain of human Rad51D
Int.J.Biochem.Cell Biol., 43:416-422, 2011

PubMed Abstract: Rad51D, one of five Rad51 paralogs, is required for homologous recombination and disruption of Holliday junctions with bloom syndrome protein (BLM) in vertebrates. The N-terminal domain of Rad51D is highly conserved in eukaryotic Rad51D orthologs and is essential for protein-protein interaction with XRCC2, but nothing is known about its individual structure or function. In this study, we determined the solution structure of the human Rad51D N-terminal domain (residues 1-83), which consists of four short helices flanked by long N- and C-terminal tails. Interestingly, the position of the N-terminal tail (residues 1-13) is fixed within the domain structure via several hydrophobic interactions between Leu4 and Thr27, Leu4 and Val28, and Val6 and Ile17. We show that the domain preferentially binds to ssDNA versus dsDNA and does not bind to a mobile Holliday junction by electrophoretic mobility shift assay. NMR titration and dynamics studies showed that human Rad51D-N interacts with ssDNA by positively charged and hydrophobic residues on its surface. The results suggest that the N-terminal domain of Rad51D is required for the ssDNA-specific binding function of human Rad51D and that the conserved N-terminal domains of other Rad51 paralogs may have distinguishable functions from each other in homologous recombination.

PubMed: 21111057
DOI: 10.1016/j.biocel.2010.11.014

Experimental method

SOLUTION NMR