1IV1

Structure of 2C-Methyl-D-erythritol-2,4-cyclodiphosphate Synthase

1IV1 の概要

• エントリーDOI: 10.2210/pdb1iv1/pdb
• 関連するPDBエントリー: 1IV2 1IV3 1IV4
• 分子名称: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (2 entities in total)
• 機能のキーワード: isoprenoid, non-mevalonate, synthase, riken structural genomics/proteomics initiative, rsgi, structural genomics, lyase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 99264.47

構造登録者

Kishida, H.,Wada, T.,Unzai, S.,Kuzuyama, T.,Terada, T.,Sirouzu, M.,Yokoyama, S.,Tame, J.R.H.,Park, S.-Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2002-03-11, 公開日: 2002-09-11, 最終更新日: 2023-12-27)

主引用文献

Kishida, H.,Wada, T.,Unzai, S.,Kuzuyama, T.,Takagi, M.,Terada, T.,Shirouzu, M.,Yokoyama, S.,Tame, J.R.,Park, S.Y.
Structure and catalytic mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) synthase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.
Acta Crystallogr.,Sect.D, 59:23-31, 2003

PubMed Abstract: Precursors for isoprenoid synthesis are essential in all organisms. These compounds are synthesized by one of two known routes: the well characterized mevalonate pathway or a recently discovered non-mevalonate route which is used in many bacteria and human pathogens. Since the second pathway is both vital and unlike any found in humans, enzymes catalysing reactions along this synthetic route are possible drug targets. The structure of one such enzyme from the thermophilic bacterium Thermus thermophilus has been solved to high resolution in the presence of substrate and with a substrate analogue. Enzyme co-crystallized with substrate shows only one product, cytosine monophosphate (CMP), in the active site. At the high resolution of the refinement (1.6 A) the positions and coordination of the magnesium ions in the active site are clearly seen.

PubMed: 12499535
DOI: 10.1107/S0907444902017705

実験手法

X-RAY DIFFRACTION (1.65 Å)