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Literature summary extracted from

  • Richard, S.B.; Ferrer, J.L.; Bowman, M.E.; Lillo, A.M.; Tetzlaff, C.N.; Cane, D.E.; Noel, J.P.
    Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway (2002), J. Biol. Chem., 277, 8667-8672.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.6.1.12 hanging-drop vapour diffusion method, X-ray crystal structures refined to 2.8 A resolution. The first structure contains a bound Mn2+ cation and the second structure contains CMP, 2-C-methyl-D-erythritol-2,4-cyclodiphosphate, and Mn2+ Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.12 additional information the tetrahedrally arranged transition metal binding site, potentially occupied by Mn2+, sits at the base of the active site cleft. A phosphate oxygen of 2-C-methyl-D-erythritol-2,4-cyclodiphosphate and the side chains of Asp8, His10, and His42 occupy the metal side chains of Asp8, His10, and His42 occupy the metal side coordination sphere Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.12 Escherichia coli P62617
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.12
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.12 2-phospho-4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol
-
 Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate + CMP
-
 ?

Subunits

EC Number Subunits Comment Organism
4.6.1.12 trimer homotrimeric quarternary structure built around a central hydrophobic cavity and three externally facing active sites Escherichia coli