5NWL
Crystal structure of a human RAD51-ATP filament.
Summary for 5NWL
| Entry DOI | 10.2210/pdb5nwl/pdb |
| Descriptor | DNA repair protein RAD51 homolog 1, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | atpase, dna-strand exchange, homologous recombination, double-strand dna break repair, recombination |
| Biological source | Homo sapiens (Human) |
| Cellular location | Nucleus : Q06609 |
| Total number of polymer chains | 14 |
| Total formula weight | 525568.55 |
| Authors | Pellegrini, L.,Moschetti, T. (deposition date: 2017-05-06, release date: 2018-03-07, Last modification date: 2024-01-17) |
| Primary citation | Brouwer, I.,Moschetti, T.,Candelli, A.,Garcin, E.B.,Modesti, M.,Pellegrini, L.,Wuite, G.J.,Peterman, E.J. Two distinct conformational states define the interaction of human RAD51-ATP with single-stranded DNA. EMBO J., 37:-, 2018 Cited by PubMed Abstract: An essential mechanism for repairing DNA double-strand breaks is homologous recombination (HR). One of its core catalysts is human RAD51 (hRAD51), which assembles as a helical nucleoprotein filament on single-stranded DNA, promoting DNA-strand exchange. Here, we study the interaction of hRAD51 with single-stranded DNA using a single-molecule approach. We show that ATP-bound hRAD51 filaments can exist in two different states with different contour lengths and with a free-energy difference of ~4 kT per hRAD51 monomer. Upon ATP hydrolysis, the filaments convert into a disassembly-competent ADP-bound configuration. In agreement with the single-molecule analysis, we demonstrate the presence of two distinct protomer interfaces in the crystal structure of a hRAD51-ATP filament, providing a structural basis for the two conformational states of the filament. Together, our findings provide evidence that hRAD51-ATP filaments can exist in two interconvertible conformational states, which might be functionally relevant for DNA homology recognition and strand exchange. PubMed: 29507080DOI: 10.15252/embj.201798162 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.93 Å) |
Structure validation
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