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2UZH

Mycobacterium smegmatis 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase (IspF)

Summary for 2UZH
Entry DOI10.2210/pdb2uzh/pdb
Descriptor2C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, ZINC ION, CYTIDINE-5'-DIPHOSPHATE, ... (9 entities in total)
Functional Keywordsispf, lyase, mycobacteria, complex with cdp, non-mevalonate pathway of isoprenoid biosynthesis
Biological sourceMYCOBACTERIUM SMEGMATIS
Total number of polymer chains3
Total formula weight52600.31
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 citationBuetow, 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: 17956607
DOI: 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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