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| | <StructureSection load='5jx8' size='340' side='right'caption='[[5jx8]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5jx8' size='340' side='right'caption='[[5jx8]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jx8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccw Vaccw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jx8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_WR Vaccinia virus WR]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JX8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jx0|5jx0]], [[5jx3|5jx3]]</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">UNG, TS17, VACWR109, D4R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10254 VACCW])</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=5jx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jx8 OCA], [https://pdbe.org/5jx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jx8 RCSB], [https://www.ebi.ac.uk/pdbsum/5jx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jx8 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uracil-DNA_glycosylase Uracil-DNA glycosylase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jx8 OCA], [http://pdbe.org/5jx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jx8 RCSB], [http://www.ebi.ac.uk/pdbsum/5jx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jx8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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 WR]] |
| - | [[Category: Vaccw]]
| + | [[Category: Chattopadhyay D]] |
| - | [[Category: Chattopadhyay, D]] | + | [[Category: Schormann N]] |
| - | [[Category: Schormann, N]] | + | |
| - | [[Category: Dna repair enzyme component of processivity factor poxvirus]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| 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
Uracil-DNA glycosylases are ubiquitous enzymes, which play a key role repairing damages in DNA and in maintaining genomic integrity by catalyzing the first step in the base excision repair pathway. Within the superfamily of uracil-DNA glycosylases family I enzymes or UNGs are specific for recognizing and removing uracil from DNA. These enzymes feature conserved structural folds, active site residues and use common motifs for DNA binding, uracil recognition and catalysis. Within this family the enzymes of poxviruses are unique and most remarkable in terms of amino acid sequences, characteristic motifs and more importantly for their novel non-enzymatic function in DNA replication. UNG of vaccinia virus, also known as D4, is the most extensively characterized UNG of the poxvirus family. D4 forms an unusual heterodimeric processivity factor by attaching to a poxvirus-specific protein A20, which also binds to the DNA polymerase E9 and recruits other proteins necessary for replication. D4 is thus integrated in the DNA polymerase complex, and its DNA-binding and DNA scanning abilities couple DNA processivity and DNA base excision repair at the replication fork. The adaptations necessary for taking on the new function are reflected in the amino acid sequence and the three-dimensional structure of D4. An overview of the current state of the knowledge on the structure-function relationship of D4 is provided here.
Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases.,Schormann N, Zhukovskaya N, Bedwell G, Nuth M, Gillilan R, Prevelige PE, Ricciardi RP, Banerjee S, Chattopadhyay D Protein Sci. 2016 Dec;25(12):2113-2131. doi: 10.1002/pro.3058. Epub 2016 Nov 2. PMID:27684934[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schormann N, Zhukovskaya N, Bedwell G, Nuth M, Gillilan R, Prevelige PE, Ricciardi RP, Banerjee S, Chattopadhyay D. Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases. Protein Sci. 2016 Dec;25(12):2113-2131. doi: 10.1002/pro.3058. Epub 2016 Nov 2. PMID:27684934 doi:http://dx.doi.org/10.1002/pro.3058
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