1u3p
IspF native
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OverviewOverview
Isoprenoids are biosynthesized from isopentenyl diphosphate and the, isomeric dimethylallyl diphosphate via the mevalonate pathway or a, mevalonate-independent pathway that was identified during the last decade., The non-mevalonate pathway is present in many bacteria, some algae and in, certain protozoa such as the malaria parasite Plasmodium falciparum and in, the plastids of higher plants, but not in mammals and archaea. Therefore, these enzymes have been recognised as promising drug targets. We report, the crystal structure of Escherichia coli 2C-, methyl-d-erythritol-2,4-cyclodiphosphate synthase (IspF), which converts, 4-diphosphocytidyl-2C-methyl-d-erythritol 2-phosphate into, 2C-methyl-d-erythritol 2,4-cyclodiphosphate and CMP in a Mg-dependent, reaction. The protein forms homotrimers that tightly bind one zinc ion per, subunit at the active site, which helps to position the substrate for, direct attack of the 2-phosphate group on the beta-phosphate.
About this StructureAbout this Structure
1U3P is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, with EC number 4.6.1.12 Full crystallographic information is available from OCA.
ReferenceReference
Structure of 2C-methyl-d-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids., Steinbacher S, Kaiser J, Wungsintaweekul J, Hecht S, Eisenreich W, Gerhardt S, Bacher A, Rohdich F, J Mol Biol. 2002 Feb 8;316(1):79-88. PMID:11829504
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