4irb
From Proteopedia
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| - | + | ==Crystal Structure of Vaccinia Virus Uracil DNA Glycosylase Mutant del171-172D4== | |
| - | + | <StructureSection load='4irb' size='340' side='right' caption='[[4irb]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4irb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Vacca Vacca]. 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> | |
| - | ==Function== | + | </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> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2owq|2owq]], [[2owr|2owr]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACAM3000_MVA_101, CPXV_GER91_3_113, D4; UNG, MVA101R, UNG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=126794 VACCA])</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=4irb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4irb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4irb RCSB], [http://www.ebi.ac.uk/pdbsum/4irb 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. | [[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> | |
| - | == | + | ==See Also== |
| - | + | *[[Uracil-DNA glycosylase|Uracil-DNA glycosylase]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Uracil-DNA glycosylase]] | [[Category: Uracil-DNA glycosylase]] | ||
| - | [[Category: Chattopadhyay, D | + | [[Category: Vacca]] |
| - | [[Category: Nuth, M | + | [[Category: Chattopadhyay, D]] |
| - | [[Category: Ricciardi, R P | + | [[Category: Nuth, M]] |
| - | [[Category: Sartmatova, D | + | [[Category: Ricciardi, R P]] |
| - | [[Category: Schormann, N | + | [[Category: Sartmatova, D]] |
| - | [[Category: Zhukovskaya, N | + | [[Category: Schormann, N]] |
| + | [[Category: Zhukovskaya, N]] | ||
[[Category: Beta- sheets at n- and c-terminus]] | [[Category: Beta- sheets at n- and c-terminus]] | ||
[[Category: Binding partners a20 and dna]] | [[Category: Binding partners a20 and dna]] | ||
Revision as of 15:56, 24 December 2014
Crystal Structure of Vaccinia Virus Uracil DNA Glycosylase Mutant del171-172D4
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Categories: Uracil-DNA glycosylase | Vacca | Chattopadhyay, D | Nuth, M | Ricciardi, R P | Sartmatova, D | Schormann, N | Zhukovskaya, N | Beta- sheets at n- and c-terminus | Binding partners a20 and dna | Component of processivity factor | Dimeric assembly | Dna repair hydrolase | Hydrolase | Parallel beta-sheet of 4 strands in the order 2134 | Viral protein
