5jks

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m (Protected "5jks" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5jks is ON HOLD until Paper Publication
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==vaccinia virus D4 R167A mutant /A20(1-50)==
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<StructureSection load='5jks' size='340' side='right' caption='[[5jks]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
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Authors: Contesto-Richefeu, C., Tarbouriech, N., Brazzolotto, X., Burmeister, W.P., Peyrefitte, C.N., Iseni, F.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5jks]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JKS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JKS FirstGlance]. <br>
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Description: vaccinia virus D4 R167A mutant /A20(1-50)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[Category: Unreleased Structures]]
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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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[[Category: Burmeister, W.P]]
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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=5jks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jks OCA], [http://pdbe.org/5jks PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jks RCSB], [http://www.ebi.ac.uk/pdbsum/5jks PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jks ProSAT]</span></td></tr>
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[[Category: Peyrefitte, C.N]]
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/UNG_VACCC UNG_VACCC]] 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). [[http://www.uniprot.org/uniprot/A20_VACCC A20_VACCC]] Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein D4. May serve as a bridge which links the DNA polymerase E9 and the uracil DNA glycosylase (By similarity).
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__TOC__
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</StructureSection>
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[[Category: Uracil-DNA glycosylase]]
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[[Category: Brazzolotto, X]]
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[[Category: Burmeister, W P]]
[[Category: Contesto-Richefeu, C]]
[[Category: Contesto-Richefeu, C]]
[[Category: Iseni, F]]
[[Category: Iseni, F]]
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[[Category: Brazzolotto, X]]
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[[Category: Peyrefitte, C N]]
[[Category: Tarbouriech, N]]
[[Category: Tarbouriech, N]]
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[[Category: Dna binding]]
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[[Category: Dna polymerase binding]]
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[[Category: Dna polymerase processivity factor]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-replication complex]]

Revision as of 15:33, 14 September 2016

vaccinia virus D4 R167A mutant /A20(1-50)

5jks, resolution 2.79Å

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