5iwx

Crystal structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from Bacillus subtitis

spinqualitylabelsall models 5iwx, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5iwx is a 6 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.99Å Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ISPF_BACSU Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). Publication Abstract from PubMed 2-C-methyl-d-erythritol 2, 4-cyclodiphosphate synthase (IspF) is a key enzyme in the 2-C-Methyl-d-erythritol-4-phosphate (MEP) pathway of isoprenoid biosynthesis. This enzyme catalyzes the 4-diphosphocytidyl-2-C-methyl-d-erythritol 2-phosphate (CDPME2P) to 2-C-methyl-d-erythritol 2, 4-cyclodiphosphate (MEcDP) with concomitant release of cytidine 5'-diphospate (cytosine monophosphate) (CMP). Bacillus subtilis is a potential host cell for the production of isoprenoids, but few studies are performed on the key enzymes of MEP pathway in B. subtilis In this work, the high resolution crystal structures of IspF in native and complex with CMP from B. subtilis have been determinated. Structural comparisons indicate that there is a looser packing of the subunits of IspF in B. subtilis , whereas the solvent accessible surface of its active pockets is smaller than that in Escherichia coli. Meanwhile, the protein-protein associations of 2-C-Methyl-d-erythritol-4-phosphatecytidyltransferase (IspD), 4-diphosphocytidyl-2-C-methyl-d-erythritol kinase (IspE) and IspF from B. subtilis and E. coli , which catalyze three consecutive steps in the MEP pathway, are analyzed by native gel shift and size exclusion chromatography methods. The data here shows that protein complex assembly is not detectable. These results will be useful for isoprenoid biosynthesis by metabolic engineering. Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly among IspD/IspE/IspF enzymes in the MEP pathway.,Liu Z, Jin Y, Liu W, Tao Y, Wang G Biosci Rep. 2018 Jan 15. pii: BSR20171370. doi: 10.1042/BSR20171370. PMID:29335298 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also MECDP synthase 3D structures

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