6s1o: Difference between revisions
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==Human polymerase delta holoenzyme Conformer 3== | |||
<SX load='6s1o' size='340' side='right' viewer='molstar' caption='[[6s1o]], [[Resolution|resolution]] 8.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6s1o]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S1O FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOC:2,3-DIDEOXYCYTIDINE-5-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6s1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s1o OCA], [https://pdbe.org/6s1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s1o RCSB], [https://www.ebi.ac.uk/pdbsum/6s1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s1o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DPOD3_HUMAN DPOD3_HUMAN] Required for optimal DNA polymerase delta activity.<ref>PMID:10219083</ref> <ref>PMID:10852724</ref> <ref>PMID:16510448</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In eukaryotes, DNA polymerase delta (Pol delta) bound to the proliferating cell nuclear antigen (PCNA) replicates the lagging strand and cooperates with flap endonuclease 1 (FEN1) to process the Okazaki fragments for their ligation. We present the high-resolution cryo-EM structure of the human processive Pol delta-DNA-PCNA complex in the absence and presence of FEN1. Pol delta is anchored to one of the three PCNA monomers through the C-terminal domain of the catalytic subunit. The catalytic core sits on top of PCNA in an open configuration while the regulatory subunits project laterally. This arrangement allows PCNA to thread and stabilize the DNA exiting the catalytic cleft and recruit FEN1 to one unoccupied monomer in a toolbelt fashion. Alternative holoenzyme conformations reveal important functional interactions that maintain PCNA orientation during synthesis. This work sheds light on the structural basis of Pol delta's activity in replicating the human genome. | |||
Structure of the processive human Pol delta holoenzyme.,Lancey C, Tehseen M, Raducanu VS, Rashid F, Merino N, Ragan TJ, Savva CG, Zaher MS, Shirbini A, Blanco FJ, Hamdan SM, De Biasio A Nat Commun. 2020 Feb 28;11(1):1109. doi: 10.1038/s41467-020-14898-6. PMID:32111820<ref>PMID:32111820</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6s1o" 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/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: De Biasio A]] | |||
[[Category: Hamdan SM]] | |||
[[Category: Lancey C]] |
Latest revision as of 13:13, 22 May 2024
Human polymerase delta holoenzyme Conformer 3Human polymerase delta holoenzyme Conformer 3
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