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8oj7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==HSV-1 DNA polymerase-processivity factor complex in halted elongation state== | |
| - | + | <StructureSection load='8oj7' size='340' side='right'caption='[[8oj7]], [[Resolution|resolution]] 2.46Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8oj7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_KOS Human alphaherpesvirus 1 strain KOS] 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=8OJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OJ7 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]] 2.46Å</td></tr> | |
| - | [[Category: | + | <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=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8oj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oj7 OCA], [https://pdbe.org/8oj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oj7 RCSB], [https://www.ebi.ac.uk/pdbsum/8oj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oj7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DPOL_HHV11 DPOL_HHV11] Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5' to 3' direction. Therefore, it can catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during viral DNA replication.<ref>PMID:2553735</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human alphaherpesvirus 1 strain KOS]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Elias P]] | ||
| + | [[Category: Grunewald K]] | ||
| + | [[Category: Gustavsson E]] | ||
| + | [[Category: Hallberg BM]] | ||
Current revision
HSV-1 DNA polymerase-processivity factor complex in halted elongation state
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