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TitleThe Flexible Motif V of Epstein-Barr Virus Deoxyuridine 5'-Triphosphate Pyrophosphatase is Essential for Catalysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 284, Page 25280-, Year 2009
Publish dateMar 27, 2009 (structure data deposition date)
AuthorsFreeman, L. / Buisson, M. / Tarbouriech, N. / Van Der Heyden, A. / Labbe, P. / Burmeister, W.P.
External linksJ. Biol. Chem. / PubMed:19586911
MethodsX-ray diffraction
Resolution1.5 - 2.01 Å
Structure data

PDB-2we0:
EBV dUTPase mutant Cys4Ser
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-2we1:
EBV dUTPase mutant Asp131Asn with bound dUMP
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2we2:
EBV dUTPase double mutant Gly78Asp-Asp131Ser with dUMP
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-2we3:
EBV dUTPase inactive mutant deleted of motif V
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

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

ChemComp-SO4:
SULFATE ION

ChemComp-TEO:
MALATE LIKE INTERMEDIATE

ChemComp-HOH:
WATER

ChemComp-DUT:
DEOXYURIDINE-5'-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

Source
  • human herpesvirus 4 (Epstein-Barr virus)
KeywordsHYDROLASE / DUTPASE / MONOMER / HUMAN HERPES VIRUS / EPSTEIN-BARR VIRUS / NUCLEOTIDE METABOLISM / PYROPHOSPHATASE / HERPES VIRUS

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