2PMP

Structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from the isoprenoid biosynthetic pathway of Arabidopsis thaliana

2PMP の概要

• エントリーDOI: 10.2210/pdb2pmp/pdb
• 関連するPDBエントリー: 1GX1 1IV1 1JN1
• 分子名称: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, ZINC ION, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: plant enzymes, arabidopsis thaliana, mep pathway, isoprenoid-binding proteins, cmp, zinc ions, lyase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• 細胞内の位置: Plastid, chloroplast stroma : Q9CAK8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17868.11

構造登録者

Calisto, B.M.,Perez-Gil, J.,Querol-Audi, J.,Fita, I.,Imperial, S. (登録日: 2007-04-23, 公開日: 2007-09-18, 最終更新日: 2023-08-30)

主引用文献

Calisto, B.M.,Perez-Gil, J.,Bergua, M.,Querol-Audi, J.,Fita, I.,Imperial, S.
Biosynthesis of isoprenoids in plants: Structure of the 2C-methyl-D-erithrytol 2,4-cyclodiphosphate synthase from Arabidopsis thaliana. Comparison with the bacterial enzymes.
Protein Sci., 16:2082-2088, 2007

PubMed Abstract: The X-ray crystal structure of the 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (MCS) from Arabidopsis thaliana has been solved at 2.3 A resolution in complex with a cytidine-5-monophosphate (CMP) molecule. This is the first structure determined of an MCS enzyme from a plant. Major differences between the A. thaliana and bacterial MCS structures are found in the large molecular cavity that forms between subunits and involve residues that are highly conserved among plants. In some bacterial enzymes, the corresponding cavity has been shown to be an isoprenoid diphosphate-like binding pocket, with a proposed feedback-regulatory role. Instead, in the structure from A. thaliana the cavity is unsuited for binding a diphosphate moiety, which suggests a different regulatory mechanism of MCS enzymes between bacteria and plants.

PubMed: 17660251
DOI: 10.1110/ps.072972807

実験手法

X-RAY DIFFRACTION (2.3 Å)