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5jx0

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==Temperature sensitive D4 mutant L110F==
==Temperature sensitive D4 mutant L110F==
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<StructureSection load='5jx0' size='340' side='right' caption='[[5jx0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5jx0' size='340' side='right'caption='[[5jx0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jx0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JX0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JX0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jx0]] is a 4 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=5JX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JX0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jx3|5jx3]], [[5jx8|5jx8]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jx0 OCA], [https://pdbe.org/5jx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jx0 RCSB], [https://www.ebi.ac.uk/pdbsum/5jx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jx0 ProSAT]</span></td></tr>
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<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=5jx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jx0 OCA], [http://pdbe.org/5jx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jx0 RCSB], [http://www.ebi.ac.uk/pdbsum/5jx0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jx0 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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).
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:27684934</ref>
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==See Also==
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*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5jx0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Uracil-DNA glycosylase]]
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[[Category: Large Structures]]
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[[Category: Chattopadhyay, D]]
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[[Category: Vaccinia virus WR]]
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[[Category: Schormann, N]]
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[[Category: Chattopadhyay D]]
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[[Category: Dna repair enzyme component of processivity factor poxvirus l110f mutant]]
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[[Category: Schormann N]]
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[[Category: Hydrolase]]
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Current revision

Temperature sensitive D4 mutant L110F

PDB ID 5jx0

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