1SZP
A Crystal Structure of the Rad51 Filament
Summary for 1SZP
| Entry DOI | 10.2210/pdb1szp/pdb |
| Descriptor | DNA repair protein RAD51, SULFATE ION (2 entities in total) |
| Functional Keywords | homologous recombination, asymmetry, rad51 filament, dna binding protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: P25454 |
| Total number of polymer chains | 6 |
| Total formula weight | 209988.61 |
| Authors | Conway, A.B.,Lynch, T.W.,Zhang, Y.,Fortin, G.S.,Symington, L.S.,Rice, P.A. (deposition date: 2004-04-06, release date: 2004-07-13, Last modification date: 2023-08-23) |
| Primary citation | Conway, A.B.,Lynch, T.W.,Zhang, Y.,Fortin, G.S.,Fung, C.W.,Symington, L.S.,Rice, P.A. Crystal structure of a Rad51 filament. Nat.Struct.Mol.Biol., 11:791-796, 2004 Cited by PubMed Abstract: Rad51, the major eukaryotic homologous recombinase, is important for the repair of DNA damage and the maintenance of genomic diversity and stability. The active form of this DNA-dependent ATPase is a helical filament within which the search for homology and strand exchange occurs. Here we present the crystal structure of a Saccharomyces cerevisiae Rad51 filament formed by a gain-of-function mutant. This filament has a longer pitch than that seen in crystals of Rad51's prokaryotic homolog RecA, and places the ATPase site directly at a new interface between protomers. Although the filament exhibits approximate six-fold symmetry, alternate protein-protein interfaces are slightly different, implying that the functional unit of Rad51 within the filament may be a dimer. Additionally, we show that mutation of His352, which lies at this new interface, markedly disrupts DNA binding. PubMed: 15235592DOI: 10.1038/nsmb795 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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