Summary for 6E49
| Entry DOI | 10.2210/pdb6e49/pdb |
| Descriptor | Proliferating cell nuclear antigen, ATP-dependent DNA helicase PIF1 (3 entities in total) |
| Functional Keywords | complex, pcna, pif1 peptide, dna binding protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 6 |
| Total formula weight | 97782.46 |
| Authors | Buzovetsky, O.,Kwon, Y.,Pham, N.T.,Kim, C.,Ira, G.,Sung, P.,Xiong, Y. (deposition date: 2018-07-17, release date: 2018-08-22, Last modification date: 2024-03-13) |
| Primary citation | Buzovetsky, O.,Kwon, Y.,Pham, N.T.,Kim, C.,Ira, G.,Sung, P.,Xiong, Y. Role of the Pif1-PCNA Complex in Pol delta-Dependent Strand Displacement DNA Synthesis and Break-Induced Replication. Cell Rep, 21:1707-1714, 2017 Cited by PubMed Abstract: The S. cerevisiae Pif1 helicase functions with DNA polymerase (Pol) δ in DNA synthesis during break-induced replication (BIR), a conserved pathway responsible for replication fork repair and telomere recombination. Pif1 interacts with the DNA polymerase processivity clamp PCNA, but the functional significance of the Pif1-PCNA complex remains to be elucidated. Here, we solve the crystal structure of PCNA in complex with a non-canonical PCNA-interacting motif in Pif1. The structure guides the construction of a Pif1 mutant that is deficient in PCNA interaction. This mutation impairs the ability of Pif1 to enhance DNA strand displacement synthesis by Pol δ in vitro and also the efficiency of BIR in cells. These results provide insights into the role of the Pif1-PCNA-Pol δ ensemble during DNA break repair by homologous recombination. PubMed: 29141206DOI: 10.1016/j.celrep.2017.10.079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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