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| <StructureSection load='6e49' size='340' side='right'caption='[[6e49]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='6e49' size='340' side='right'caption='[[6e49]], [[Resolution|resolution]] 2.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6e49]] is a 6 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6b8i 6b8i]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E49 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6E49 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6e49]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6b8i 6b8i]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E49 FirstGlance]. <br> |
| </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6e49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e49 OCA], [http://pdbe.org/6e49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e49 RCSB], [http://www.ebi.ac.uk/pdbsum/6e49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e49 ProSAT]</span></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e49 OCA], [https://pdbe.org/6e49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e49 RCSB], [https://www.ebi.ac.uk/pdbsum/6e49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e49 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/PCNA_YEAST PCNA_YEAST]] This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.<ref>PMID:11545742</ref> <ref>PMID:12226657</ref> [[http://www.uniprot.org/uniprot/PIF1_YEAST PIF1_YEAST]] DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP. Processes at an unwinding rate of about 75 bp/s. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Involved in the maintenance of ribosomal (rDNA). Required for efficient fork arrest at the replication fork barrier within rDNA. Involved in the maintenance of mitochondrial (mtDNA). Required to maintain mtDNA under conditions that introduce dsDNA breaks in mtDNA, either preventing or repairing dsDNA breaks. May inhibit replication progression to allow time for repair. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. May have a role in conjunction with DNA2 helicase/nuclease in 5'-flap extension during Okazaki fragment processing.[HAMAP-Rule:MF_03176]<ref>PMID:10693764</ref> <ref>PMID:10926538</ref> <ref>PMID:11429610</ref> <ref>PMID:12024022</ref> <ref>PMID:15907372</ref> <ref>PMID:15923634</ref> <ref>PMID:16121131</ref> <ref>PMID:16537895</ref> <ref>PMID:16816432</ref> <ref>PMID:16878131</ref> <ref>PMID:17257907</ref> <ref>PMID:17590086</ref> <ref>PMID:17720711</ref> <ref>PMID:1849081</ref> <ref>PMID:19424434</ref> <ref>PMID:20225162</ref> <ref>PMID:21620135</ref> <ref>PMID:23175612</ref> <ref>PMID:23446274</ref> <ref>PMID:23596008</ref> <ref>PMID:23657261</ref> <ref>PMID:3038524</ref> <ref>PMID:8287473</ref> | | [https://www.uniprot.org/uniprot/PCNA_YEAST PCNA_YEAST] This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.<ref>PMID:11545742</ref> <ref>PMID:12226657</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The S. cerevisiae Pif1 helicase functions with DNA polymerase (Pol) delta 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 delta in vitro and also the efficiency of BIR in cells. These results provide insights into the role of the Pif1-PCNA-Pol delta ensemble during DNA break repair by homologous recombination.
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| Role of the Pif1-PCNA Complex in Pol delta-Dependent Strand Displacement DNA Synthesis and Break-Induced Replication.,Buzovetsky O, Kwon Y, Pham NT, Kim C, Ira G, Sung P, Xiong Y Cell Rep. 2017 Nov 14;21(7):1707-1714. doi: 10.1016/j.celrep.2017.10.079. PMID:29141206<ref>PMID:29141206</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6e49" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Buzovetsky, O]] | | [[Category: Saccharomyces cerevisiae S288C]] |
| [[Category: Ira, G]] | | [[Category: Buzovetsky O]] |
| [[Category: Kim, C]] | | [[Category: Ira G]] |
| [[Category: Kwon, Y]] | | [[Category: Kim C]] |
| [[Category: Pham, N T]] | | [[Category: Kwon Y]] |
| [[Category: Sung, P]] | | [[Category: Pham NT]] |
| [[Category: Xiong, Y]] | | [[Category: Sung P]] |
| [[Category: Complex]]
| | [[Category: Xiong Y]] |
| [[Category: Dna binding protein]]
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| [[Category: Pcna]]
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| [[Category: Pif1 peptide]]
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