2UZH
Mycobacterium smegmatis 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase (IspF)
Summary for 2UZH
Entry DOI | 10.2210/pdb2uzh/pdb |
Descriptor | 2C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, ZINC ION, CYTIDINE-5'-DIPHOSPHATE, ... (9 entities in total) |
Functional Keywords | ispf, lyase, mycobacteria, complex with cdp, non-mevalonate pathway of isoprenoid biosynthesis |
Biological source | MYCOBACTERIUM SMEGMATIS |
Total number of polymer chains | 3 |
Total formula weight | 52600.31 |
Authors | Buetow, L.,Brown, A.C.,Parish, T.,Hunter, W.N. (deposition date: 2007-04-27, release date: 2007-11-06, Last modification date: 2023-12-13) |
Primary citation | Buetow, L.,Brown, A.C.,Parish, T.,Hunter, W.N. The Structure of Mycobacteria 2C-Methyl-D-Erythritol-2,4-Cyclodiphosphate Synthase, an Essential Enzyme, Provides a Platform for Drug Discovery. Bmc Struct.Biol., 7:68-, 2007 Cited by PubMed Abstract: The prevalence of tuberculosis, the prolonged and expensive treatment that this disease requires and an increase in drug resistance indicate an urgent need for new treatments. The 1-deoxy-D-xylulose 5-phosphate pathway of isoprenoid precursor biosynthesis is an attractive chemotherapeutic target because it occurs in many pathogens, including Mycobacterium tuberculosis, and is absent from humans. To underpin future drug development it is important to assess which enzymes in this biosynthetic pathway are essential in the actual pathogens and to characterize them. PubMed: 17956607DOI: 10.1186/1472-6807-7-68 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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