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| | <StructureSection load='3nt7' size='340' side='right'caption='[[3nt7]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3nt7' size='340' side='right'caption='[[3nt7]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nt7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_western_reserve Vaccinia virus western reserve]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NT7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nt7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Western_Reserve Vaccinia virus Western Reserve]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NT7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2owq|2owq]], [[2owr|2owr]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D4R, VACWR109 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=696871 Vaccinia virus Western Reserve])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Uracil-DNA_glycosylase Uracil-DNA glycosylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.27 3.2.2.27] </span></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=3nt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nt7 OCA], [https://pdbe.org/3nt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nt7 RCSB], [https://www.ebi.ac.uk/pdbsum/3nt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nt7 ProSAT]</span></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=3nt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nt7 OCA], [https://pdbe.org/3nt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nt7 RCSB], [https://www.ebi.ac.uk/pdbsum/3nt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nt7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/UNG_VACCA UNG_VACCA]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA.
| + | [https://www.uniprot.org/uniprot/UNG_VACCW UNG_VACCW] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Uracil-DNA glycosylase]]
| + | [[Category: Vaccinia virus Western Reserve]] |
| - | [[Category: Vaccinia virus western reserve]] | + | [[Category: Chattopadhyay D]] |
| - | [[Category: Chattopadhyay, D]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Uracil-dna glycosylase fold]]
| + | |
| Structural highlights
Function
UNG_VACCW Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA (By similarity).
Publication Abstract from PubMed
Genome replication is inefficient without processivity factors, which tether DNA polymerases to their templates. The vaccinia virus DNA polymerase E9 requires two viral proteins, A20 and D4, for processive DNA synthesis, yet the mechanism of how this tricomplex functions is unknown. This study confirms that these three proteins are necessary and sufficient for processivity, and it focuses on the role of D4, which also functions as a uracil DNA glycosylase (UDG) repair enzyme. A series of D4 mutants was generated to discover which sites are important for processivity. Three point mutants (K126V, K160V, and R187V) which did not function in processive DNA synthesis, though they retained UDG catalytic activity, were identified. The mutants were able to compete with wild-type D4 in processivity assays and retained binding to both A20 and DNA. The crystal structure of R187V was resolved and revealed that the local charge distribution around the substituted residue is altered. However, the mutant protein was shown to have no major structural distortions. This suggests that the positive charges of residues 126, 160, and 187 are required for D4 to function in processive DNA synthesis. Consistent with this is the ability of the conserved mutant K126R to function in processivity. These mutants may help unlock the mechanism by which D4 contributes to processive DNA synthesis.
Vaccinia virus D4 mutants defective in processive DNA synthesis retain binding to A20 and DNA.,Druck Shudofsky AM, Silverman JE, Chattopadhyay D, Ricciardi RP J Virol. 2010 Dec;84(23):12325-35. Epub 2010 Sep 22. PMID:20861259[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Druck Shudofsky AM, Silverman JE, Chattopadhyay D, Ricciardi RP. Vaccinia virus D4 mutants defective in processive DNA synthesis retain binding to A20 and DNA. J Virol. 2010 Dec;84(23):12325-35. Epub 2010 Sep 22. PMID:20861259 doi:10.1128/JVI.01435-10
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