1JY8
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (IspF)
1JY8 の概要
エントリーDOI | 10.2210/pdb1jy8/pdb |
分子名称 | 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, ZINC ION, CYTIDINE-5'-MONOPHOSPHATE, ... (5 entities in total) |
機能のキーワード | isoprenoid biosynthesis; terpenes; malaria; drug design, biosynthetic protein |
由来する生物種 | Escherichia coli |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 17587.23 |
構造登録者 | Steinbacher, S.,Kaiser, J.,Wungsintaweekul, J.,Hecht, S.,Eisenreich, W.,Gerhardt, S.,Bacher, A.,Rohdich, F. (登録日: 2001-09-11, 公開日: 2002-01-30, 最終更新日: 2024-02-07) |
主引用文献 | Steinbacher, S.,Kaiser, J.,Wungsintaweekul, J.,Hecht, S.,Eisenreich, W.,Gerhardt, S.,Bacher, A.,Rohdich, F. Structure of 2C-methyl-d-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids. J.Mol.Biol., 316:79-88, 2002 Cited by PubMed Abstract: 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. PubMed: 11829504DOI: 10.1006/jmbi.2001.5341 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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