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Structure paper

TitleStructure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis.
Journal, issue, pagesStructure, Vol. 15, Page 1014-1022, Year 2007
Publish dateNov 28, 2006 (structure data deposition date)
AuthorsGabelli, S.B. / Bianchet, M.A. / Xu, W. / Dunn, C.A. / Niu, Z.D. / Amzel, L.M. / Bessman, M.J.
External linksStructure / PubMed:17698004
MethodsX-ray diffraction
Resolution1.8 - 2.6 Å
Structure data

PDB-2o1c:
Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2o5w:
Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase in complex with Sm+3 and pyrophosphate
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-PPV:
PYROPHOSPHATE

ChemComp-HOH:
WATER

ChemComp-SM:
SAMARIUM (III) ION

ChemComp-NA:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Nudix NTP hydrolase NTP pyrophosphohydrolase MutT dihydroneopterin triphosphate pyrophosphohydrolase folate biosynthesis / dihydroneopterin triphosphate pyrophosphohydrolase nudix nucleoside triphosphate pyrophosphohydrolase mutt

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