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TitleMechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 2815-2824, Year 2014
Publish dateJul 19, 2013 (structure data deposition date)
AuthorsVorontsov, I.I. / Wu, Y. / Delucia, M. / Minasov, G. / Mehrens, J. / Shuvalova, L. / Anderson, W.F. / Ahn, J.
External linksJ. Biol. Chem. / PubMed:24338016
MethodsX-ray diffraction
Resolution2.35 Å
Structure data

PDB-4lrl:
Structure of an Enterococcus Faecalis HD-domain protein complexed with dGTP and dTTP
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

ChemComp-DGT:
2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-TTP:
THYMIDINE-5'-TRIPHOSPHATE

ChemComp-MLI:
MALONATE ION

ChemComp-HOH:
WATER

Source
  • enterococcus faecalis (bacteria)
KeywordsHYDROLASE / Structural Genomics / PSI-2 / Protein Structure Initiative / Midwest Center for Structural Genomics / MCSG / HD Domain / Phosphohydrolase / dNTPase / Allosteric Regulation / METAL BINDING PROTEIN

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