View source for 5jkt


==vaccinia virus D4 P173G mutant /A20(1-50)==
<StructureSection load='5jkt' size='340' side='right'caption='[[5jkt]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jkt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Copenhagen Vaccinia virus Copenhagen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JKT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5jkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jkt OCA], [https://pdbe.org/5jkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jkt RCSB], [https://www.ebi.ac.uk/pdbsum/5jkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jkt ProSAT]</span></td></tr>
</table>
== Function ==
[https://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).
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== Publication Abstract from PubMed ==
The Vaccinia virus polymerase holoenzyme is composed of three subunits: E9, the catalytic DNA polymerase subunit; D4, a uracil-DNA glycosylase; and A20, a protein with no known enzymatic activity. The D4/A20 heterodimer is the DNA polymerase cofactor, the function of which is essential for processive DNA synthesis. The recent crystal structure of D4 bound to the first 50 amino acids of A20 (D4/A201-50) revealed the importance of three residues, forming a cation-pi interaction at the dimerization interface, for complex formation. These are Arg167 and Pro173 of D4 and Trp43 of A20. Here, the crystal structures of the three mutants D4-R167A/A201-50, D4-P173G/A201-50 and D4/A201-50-W43A are presented. The D4/A20 interface of the three structures has been analysed for atomic solvation parameters and cation-pi interactions. This study confirms previous biochemical data and also points out the importance for stability of the restrained conformational space of Pro173. Moreover, these new structures will be useful for the design and rational improvement of known molecules targeting the D4/A20 interface.

Structural analysis of point mutations at the Vaccinia virus A20/D4 interface.,Contesto-Richefeu C, Tarbouriech N, Brazzolotto X, Burmeister WP, Peyrefitte CN, Iseni F Acta Crystallogr F Struct Biol Commun. 2016 Sep;72(Pt 9):687-91. doi:, 10.1107/S2053230X16011778. Epub 2016 Aug 9. PMID:27599859<ref>PMID:27599859</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5jkt" style="background-color:#fffaf0;"></div>

==See Also==
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vaccinia virus Copenhagen]]
[[Category: Brazzolotto X]]
[[Category: Burmeister WP]]
[[Category: Contesto-Richefeu C]]
[[Category: Iseni F]]
[[Category: Peyrefitte CN]]
[[Category: Tarbouriech N]]