4irb

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<StructureSection load='4irb' size='340' side='right'caption='[[4irb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='4irb' size='340' side='right'caption='[[4irb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4irb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus_western_reserve Vaccinia virus western reserve]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IRB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4irb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Western_Reserve Vaccinia virus Western Reserve]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IRB 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2owq|2owq]], [[2owr|2owr]]</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D4R, VACWR109 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=696871 Vaccinia virus Western Reserve])</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=4irb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4irb OCA], [https://pdbe.org/4irb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4irb RCSB], [https://www.ebi.ac.uk/pdbsum/4irb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4irb ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4irb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4irb OCA], [http://pdbe.org/4irb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4irb RCSB], [http://www.ebi.ac.uk/pdbsum/4irb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4irb ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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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).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== 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.
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.
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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>
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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:023519808<ref>PMID:023519808</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Uracil-DNA glycosylase]]
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[[Category: Vaccinia virus Western Reserve]]
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[[Category: Vaccinia virus western reserve]]
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[[Category: Chattopadhyay D]]
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[[Category: Chattopadhyay, D]]
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[[Category: Nuth M]]
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[[Category: Nuth, M]]
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[[Category: Ricciardi RP]]
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[[Category: Ricciardi, R P]]
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[[Category: Sartmatova D]]
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[[Category: Sartmatova, D]]
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[[Category: Schormann N]]
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[[Category: Schormann, N]]
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[[Category: Zhukovskaya N]]
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[[Category: Zhukovskaya, N]]
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[[Category: Beta- sheets at n- and c-terminus]]
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[[Category: Binding partners a20 and dna]]
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[[Category: Component of processivity factor]]
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[[Category: Dimeric assembly]]
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[[Category: Dna repair hydrolase]]
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[[Category: Hydrolase]]
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[[Category: Parallel beta-sheet of 4 strands in the order 2134]]
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[[Category: Viral protein]]
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Current revision

Crystal Structure of Vaccinia Virus Uracil DNA Glycosylase Mutant del171-172D4

PDB ID 4irb

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