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TitleStructure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway.
Journal, issue, pagesJ. Biol. Chem., Vol. 277, Page 8667-8672, Year 2002
Publish dateDec 18, 2001 (structure data deposition date)
AuthorsRichard, S.B. / Ferrer, J.L. / Bowman, M.E. / Lillo, A.M. / Tetzlaff, C.N. / Cane, D.E. / Noel, J.P.
External linksJ. Biol. Chem. / PubMed:11786530
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-1knj:
Co-Crystal Structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate Synthase (ispF) from E. coli Involved in Mevalonate-Independent Isoprenoid Biosynthesis, Complexed with CMP/MECDP/Mn2+
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-1knk:
Crystal Structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate Synthase (ispF) from E. coli involved in Mevalonate-Independent Isoprenoid Biosynthesis
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-C5P:
CYTIDINE-5'-MONOPHOSPHATE

ChemComp-CDI:
2C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsMETAL BINDING PROTEIN / isoprenoids / deoxyxylulose/methyl-erythritol-phosphate pathway / cyclodiphosphate / MEP / YgbB / ispF / MECDP / 2-C-methyl-D-erythritol-2 / 4-cyclodiphosphate synthase

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