4qc9: Difference between revisions
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''' | ==Crystal structure of Vaccinia virus uracil-DNA glycosylase mutant 3GD4== | ||
<StructureSection load='4qc9' size='340' side='right' caption='[[4qc9]], [[Resolution|resolution]] 2.26Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4qc9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QC9 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dof|4dof]], [[4dog|4dog]], [[4lzb|4lzb]], [[4irb|4irb]], [[4qca|4qca]], [[4qcb|4qcb]]</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=4qc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qc9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qc9 RCSB], [http://www.ebi.ac.uk/pdbsum/4qc9 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Amino-acid residues located at a highly flexible area in the uracil DNA glycosylase of Vaccinia virus were mutated. In the crystal structure of wild-type D4 these residues lie at the dimer interface. Specifically, three mutants were generated: (i) residue Arg167 was replaced with an alanine (R167AD4), (ii) residues Glu171, Ser172 and Pro173 were substituted with three glycine residues (3GD4) and (iii) residues Glu171 and Ser172 were deleted (Delta171-172D4). Mutant proteins were expressed, purified and crystallized in order to investigate the effects of these mutations on the structure of the protein. | |||
Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase.,Sartmatova D, Nash T, Schormann N, Nuth M, Ricciardi R, Banerjee S, Chattopadhyay D Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):295-301., doi: 10.1107/S1744309113002716. Epub 2013 Feb 23. PMID:23519808<ref>PMID:23519808</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: Uracil-DNA glycosylase]] | |||
[[Category: Banerjee, S]] | [[Category: Banerjee, S]] | ||
[[Category: | [[Category: Chattopadhyay, D]] | ||
[[Category: Nash, T]] | [[Category: Nash, T]] | ||
[[Category: Nuth, M]] | [[Category: Nuth, M]] | ||
[[Category: | [[Category: Ricciardi, R]] | ||
[[Category: Sartmatova, D]] | |||
[[Category: Schormann, N]] | |||
[[Category: A20]] | |||
[[Category: Component of processivity factor]] | |||
[[Category: Dna]] | |||
[[Category: Dna repair enzyme]] | |||
[[Category: Hydrolase]] | |||
[[Category: Poxvirus]] | |||
