1w57
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STRUCTURE OF THE BIFUNCTIONAL ISPDF FROM CAMPYLOBACTER JEJUNI CONTAINING ZN
OverviewOverview
The bifunctional methylerythritol 4-phosphate cytidylyltransferase, methylerythritol 2,4-cyclodiphosphate synthase (IspDF) is unusual in that, it catalyzes nonconsecutive reactions in the 1-deoxy-D-xylulose, 5-phosphate (DOXP) pathway of isoprenoid precursor biosynthesis. The, crystal structure of IspDF from the bacterial pathogen Campylobacter, jejuni reveals an elongated hexamer with D3 symmetry compatible with the, dimeric 2C-methyl-D-erythritol-4-phosphate cytidylyltransferase and, trimeric 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase, monofunctional enzymes. Complex formation of IspDF with, 4-diphosphocytidyl-2C-methyl-D-erythritol kinase (IspE), the intervening, enzyme activity in the pathway, has been observed in solution for the, enzymes from C. jejuni and Agrobacterium ... [(full description)]
About this StructureAbout this Structure
1W57 is a [Single protein] structure of sequence from [Campylobacter jejuni] with ZN, C5P and GPP as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Hexameric assembly of the bifunctional methylerythritol 2,4-cyclodiphosphate synthase and protein-protein associations in the deoxy-xylulose-dependent pathway of isoprenoid precursor biosynthesis., Gabrielsen M, Bond CS, Hallyburton I, Hecht S, Bacher A, Eisenreich W, Rohdich F, Hunter WN, J Biol Chem. 2004 Dec 10;279(50):52753-61. Epub 2004 Oct 2. PMID:15466439
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