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TitleAnother look at the mechanism involving trimeric dUTPases in Staphylococcus aureus pathogenicity island induction involves novel players in the party.
Journal, issue, pagesNucleic Acids Res., Vol. 44, Page 5457-5469, Year 2016
Publish dateJul 2, 2015 (structure data deposition date)
AuthorsMaiques, E. / Quiles-Puchalt, N. / Donderis, J. / Ciges-Tomas, J.R. / Alite, C. / Bowring, J.Z. / Humphrey, S. / Penades, J.R. / Marina, A.
External linksNucleic Acids Res. / PubMed:27112567
MethodsX-ray diffraction
Resolution2.33 - 2.4 Å
Structure data

PDB-5cco:
Staphylococcus bacteriophage 80alpha dUTPase with dUMP.
Method: X-RAY DIFFRACTION / Resolution: 2.33 Å

PDB-5cct:
Staphylococcus bacteriophage 80alpha dUTPase G164S mutant with dUpNHpp.
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-UMP:
2'-DEOXYURIDINE 5'-MONOPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-DUP:
2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE

Source
  • staphylococcus phage 80alpha (virus)
KeywordsHYDROLASE / phage / pathogenicity island / SaPI induction / gene transfer / moonlighting proteins / Dut / dUTP / G protein / P-loop

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