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<StructureSection load='6t7y' size='340' side='right'caption='[[6t7y]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='6t7y' size='340' side='right'caption='[[6t7y]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6t7y]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6t7y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] and [https://en.wikipedia.org/wiki/Pyrococcus_abyssi_GE5 Pyrococcus abyssi GE5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T7Y FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=6t7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7y OCA], [https://pdbe.org/6t7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t7y RCSB], [https://www.ebi.ac.uk/pdbsum/6t7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7y ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PCNA_PYRAB PCNA_PYRAB] Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity). Regulates activity of NucS endonuclease and prevents non-specific cleavage.[HAMAP-Rule:MF_00317]<ref>PMID:22431731</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Replicative DNA polymerases (DNAPs) have evolved the ability to copy the genome with high processivity and fidelity. In Eukarya and Archaea, the processivity of replicative DNAPs is greatly enhanced by its binding to the proliferative cell nuclear antigen (PCNA) that encircles the DNA. We determined the cryo-EM structure of the DNA-bound PolD-PCNA complex from Pyrococcus abyssi at 3.77 A. Using an integrative structural biology approach - combining cryo-EM, X-ray crystallography, protein-protein interaction measurements, and activity assays - we describe the molecular basis for the interaction and cooperativity between a replicative DNAP and PCNA. PolD recruits PCNA via a complex mechanism, which requires two different PIP-boxes. We infer that the second PIP-box, which is shared with the eukaryotic Polalpha replicative DNAP, plays a dual role in binding either PCNA or primase, and could be a master switch between an initiation and a processive phase during replication. | |||
Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA.,Madru C, Henneke G, Raia P, Hugonneau-Beaufet I, Pehau-Arnaudet G, England P, Lindahl E, Delarue M, Carroni M, Sauguet L Nat Commun. 2020 Mar 27;11(1):1591. doi: 10.1038/s41467-020-15392-9. PMID:32221299<ref>PMID:32221299</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6t7y" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | |||
*[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pyrococcus abyssi]] | ||
[[Category: | [[Category: Pyrococcus abyssi GE5]] | ||
[[Category: Carroni | [[Category: Carroni M]] | ||
[[Category: Delarue | [[Category: Delarue M]] | ||
[[Category: | [[Category: Hugonneau Beaufet I]] | ||
[[Category: | [[Category: Madru C]] | ||
[[Category: | [[Category: Raia P]] | ||
[[Category: | [[Category: Sauguet L]] | ||
Latest revision as of 15:56, 24 January 2024
Structure of PCNA bound to cPIP motif of DP2 from P. abyssiStructure of PCNA bound to cPIP motif of DP2 from P. abyssi
Structural highlights
FunctionPCNA_PYRAB Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication (By similarity). Regulates activity of NucS endonuclease and prevents non-specific cleavage.[HAMAP-Rule:MF_00317][1] Publication Abstract from PubMedReplicative DNA polymerases (DNAPs) have evolved the ability to copy the genome with high processivity and fidelity. In Eukarya and Archaea, the processivity of replicative DNAPs is greatly enhanced by its binding to the proliferative cell nuclear antigen (PCNA) that encircles the DNA. We determined the cryo-EM structure of the DNA-bound PolD-PCNA complex from Pyrococcus abyssi at 3.77 A. Using an integrative structural biology approach - combining cryo-EM, X-ray crystallography, protein-protein interaction measurements, and activity assays - we describe the molecular basis for the interaction and cooperativity between a replicative DNAP and PCNA. PolD recruits PCNA via a complex mechanism, which requires two different PIP-boxes. We infer that the second PIP-box, which is shared with the eukaryotic Polalpha replicative DNAP, plays a dual role in binding either PCNA or primase, and could be a master switch between an initiation and a processive phase during replication. Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA.,Madru C, Henneke G, Raia P, Hugonneau-Beaufet I, Pehau-Arnaudet G, England P, Lindahl E, Delarue M, Carroni M, Sauguet L Nat Commun. 2020 Mar 27;11(1):1591. doi: 10.1038/s41467-020-15392-9. PMID:32221299[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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