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TitleMutations at the dimer interface affect both function and structure of the Vaccinia virus uracil DNA glycosylase
Journal, issue, pagesTo be Published
Publish dateJan 14, 2013 (structure data deposition date)
AuthorsSchormann, N. / Zhukovskaya, N. / Sartmatova, D. / Nuth, M. / Ricciardi, R.P. / Chattopadhyay, D.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-4irb:
Crystal Structure of Vaccinia Virus Uracil DNA Glycosylase Mutant del171-172D4
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • vaccinia virus western reserve
KeywordsHYDROLASE / Viral protein / URACIL-DNA GLYCOSYLASE FOLD IN THE CORE: 3 LAYERS (A/B/A); PARALLEL BETA-SHEET OF 4 STRANDS IN THE ORDER 2134 / BETA- SHEETS AT N- AND C-TERMINUS / DIMERIC ASSEMBLY / COMPONENT OF PROCESSIVITY FACTOR / BINDING PARTNERS A20 AND DNA / DNA REPAIR HYDROLASE

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