This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4irb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:29, 20 September 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal Structure of Vaccinia Virus Uracil DNA Glycosylase Mutant del171-172D4==
==Crystal Structure of Vaccinia Virus Uracil DNA Glycosylase Mutant del171-172D4==
-
<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 ==
-
<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>
+
<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>
-
</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>
+
</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>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2owq|2owq]], [[2owr|2owr]]</td></tr>
+
<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>
-
<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=126794 VACCA])</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=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>
-
<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://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>
+
</table>
</table>
== Function ==
== 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.
+
[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;">
+
-
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4irb" style="background-color:#fffaf0;"></div>
+
-
 
+
-
==See Also==
+
-
*[[Uracil-DNA glycosylase|Uracil-DNA glycosylase]]
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Uracil-DNA glycosylase]]
+
[[Category: Large Structures]]
-
[[Category: Vacca]]
+
[[Category: Vaccinia virus Western Reserve]]
-
[[Category: Chattopadhyay, D]]
+
[[Category: Chattopadhyay D]]
-
[[Category: Nuth, M]]
+
[[Category: Nuth M]]
-
[[Category: Ricciardi, R P]]
+
[[Category: Ricciardi RP]]
-
[[Category: Sartmatova, D]]
+
[[Category: Sartmatova D]]
-
[[Category: Schormann, N]]
+
[[Category: Schormann N]]
-
[[Category: Zhukovskaya, N]]
+
[[Category: Zhukovskaya N]]
-
[[Category: Beta- sheets at n- and c-terminus]]
+
-
[[Category: Binding partners a20 and dna]]
+
-
[[Category: Component of processivity factor]]
+
-
[[Category: Dimeric assembly]]
+
-
[[Category: Dna repair hydrolase]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Parallel beta-sheet of 4 strands in the order 2134]]
+
-
[[Category: Viral protein]]
+

Current revision

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

PDB ID 4irb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools