5IWX
Crystal structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from Bacillus subtitis
Summary for 5IWX
| Entry DOI | 10.2210/pdb5iwx/pdb |
| Related | 5IWY |
| Descriptor | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | lyase |
| Biological source | Bacillus subtilis (strain 168) |
| Total number of polymer chains | 6 |
| Total formula weight | 103031.99 |
| Authors | Liu, Z.C.,Jin, Y.,Wang, G.G. (deposition date: 2016-03-23, release date: 2017-03-29, Last modification date: 2023-11-08) |
| Primary citation | Liu, Z.C.,Jin, Y.,Liu, W.F.,Tao, Y.,Wang, G.G. Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly among IspD/IspE/IspF enzymes in the MEP pathway. Biosci. Rep., 2018 Cited by PubMed Abstract: 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 (CMP). is a potential host cell for the production of isoprenoids, but few studies are performed on the key enzymes of MEP pathway in In this work, the high-resolution crystal structures of IspF in native and complex with CMP from have been determined. Structural comparisons indicate that there is a looser packing of the subunits of IspF in , whereas the solvent accessible surface of its active pockets is smaller than that in Meanwhile, the protein-protein associations of 2-C-Methyl-d-erythritol-4-phosphatecytidyltransferase (IspD), CDPME kinase (IspE) and IspF from and , which catalyze three consecutive steps in the MEP pathway, are analyzed by native gel shift and size exclusion chromatography methods. The data here show that protein complex assembly is not detectable. These results will be useful for isoprenoid biosynthesis by metabolic engineering. PubMed: 29335298DOI: 10.1042/BSR20171370 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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