1u3l
From Proteopedia
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'''IspF with Mg and CDP''' | '''IspF with Mg and CDP''' | ||
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[[Category: Steinbacher, S.]] | [[Category: Steinbacher, S.]] | ||
[[Category: Wungsintaweekul, J.]] | [[Category: Wungsintaweekul, J.]] | ||
- | [[Category: | + | [[Category: Lyase]] |
- | [[Category: | + | [[Category: Mep pathway]] |
- | [[Category: | + | [[Category: Terpene biosynthesis]] |
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Revision as of 07:43, 3 May 2008
IspF with Mg and CDP
Overview
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 Structure
1U3L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 10:43:16 2008