5IWY

Crystal structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from Bacillus subtitis complexed with CMP and Mg2+

5IWY の概要

• エントリーDOI: 10.2210/pdb5iwy/pdb
• 関連するPDBエントリー: 5IWX
• 分子名称: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, MAGNESIUM ION, CYTIDINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 104324.78

構造登録者

Liu, Z.C.,Jin, Y.,Wang, G.G. (登録日: 2016-03-23, 公開日: 2017-03-29, 最終更新日: 2023-11-08)

主引用文献

Liu, Z.C.,Jin, Y.,Liu, W.F.,Tao, Y.,Wang, G.G.
Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly among IspD/IspE/IspF enzymes in the MEP pathway.
Biosci. Rep., 2018

PubMed Abstract: 2-C-Methyl-d-erythritol 2,4-cyclodiphosphate synthase (IspF) is a key enzyme in the 2-C-Methyl-d-erythritol-4-phosphate (MEP) pathway of isoprenoid biosynthesis. This enzyme catalyzes the 4-diphosphocytidyl-2-C-methyl-d-erythritol 2-phosphate (CDPME2P) to 2-C-methyl-d-erythritol 2,4-cyclodiphosphate (MEcDP) with concomitant release of cytidine 5'-diphospate (CMP). is a potential host cell for the production of isoprenoids, but few studies are performed on the key enzymes of MEP pathway in In this work, the high-resolution crystal structures of IspF in native and complex with CMP from have been determined. Structural comparisons indicate that there is a looser packing of the subunits of IspF in , whereas the solvent accessible surface of its active pockets is smaller than that in Meanwhile, the protein-protein associations of 2-C-Methyl-d-erythritol-4-phosphatecytidyltransferase (IspD), CDPME kinase (IspE) and IspF from and , which catalyze three consecutive steps in the MEP pathway, are analyzed by native gel shift and size exclusion chromatography methods. The data here show that protein complex assembly is not detectable. These results will be useful for isoprenoid biosynthesis by metabolic engineering.

PubMed: 29335298
DOI: 10.1042/BSR20171370

実験手法

X-RAY DIFFRACTION (1.99 Å)