4irb: Difference between revisions

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== Function ==
== Function ==
[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).
[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).
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== 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:023519808<ref>PMID:023519808</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
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Latest revision as of 10:59, 6 November 2024

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

4irb, resolution 2.30Å

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