Literature summary for 4.6.1.12 extracted from

Gabrielsen, M.; Bond, C.S.; Hallyburton, I.; Hecht, S.; Bacher, A.; Eisenreich, W.; Rohdich, F.; Hunter, W.N.
Hexameric assembly of the bifunctional methylerythritol 2,4-cyclodiphosphate synthase and protein-protein associations in the deoxy-xylulose-dependent pathway of isoprenoid precursor biosynthesis (2004), J. Biol. Chem., 279, 52753-52761.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, crystal structure of IspDF, a bifunctional methylerythritol 4-phosphate cytidyltransferase methylerythritol 2,4-cyclodidiphosphate synthase	Campylobacter jejuni

Organism

Organism	UniProt	Comment	Textmining
Agrobacterium tumefaciens	-	-	-
Campylobacter jejuni	-	-	-
Escherichia coli	P62617	-	-

Subunits

Subunits	Comment	Organism
hexamer	complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is observed in solution	Campylobacter jejuni
More	complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is observed in solution	Agrobacterium tumefaciens
More	the monofunctional enzyme 2C-methyl-D-erythritol-4-phosphate cytidyltransferase and 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase shows physical association	Escherichia coli

Synonyms

Synonyms	Comment	Organism
IspDF	bifunctional methylerythritol 4-phosphate cytidyltransferase methylerythritol 2,4-cyclodidiphosphate synthase. Complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is observed in solution	Agrobacterium tumefaciens
IspDF	bifunctional methylerythritol 4-phosphate cytidyltransferase methylerythritol 2,4-cyclodidiphosphate synthase.Complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-D-erythritol kinase is observed in solution	Campylobacter jejuni
IspE	monofunctional enzyme	Escherichia coli

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Release 2023.1 (January 2023)