2EGH

Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with a magnesium ion, NADPH and fosmidomycin

2EGH の概要

• エントリーDOI: 10.2210/pdb2egh/pdb
• 分子名称: 1-deoxy-D-xylulose 5-phosphate reductoisomerase, MAGNESIUM ION, 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID, ... (5 entities in total)
• 機能のキーワード: protein-inhibitor complex, oxidoreductase
• 由来する生物種: Escherichia coli str. K12 substr.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94253.43

構造登録者

Yajima, S.,Hara, K.,Iino, D.,Sasaki, Y.,Kuzuyama, T.,Seto, H. (登録日: 2007-03-01, 公開日: 2007-06-19, 最終更新日: 2023-10-25)

主引用文献

Yajima, S.,Hara, K.,Iino, D.,Sasaki, Y.,Kuzuyama, T.,Ohsawa, K.,Seto, H.
Structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in a quaternary complex with a magnesium ion, NADPH and the antimalarial drug fosmidomycin
Acta Crystallogr.,Sect.F, 63:466-470, 2007

PubMed Abstract: The crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) from Escherichia coli complexed with Mg(2+), NADPH and fosmidomycin was solved at 2.2 A resolution. DXR is the key enzyme in the 2-C-methyl-D-erythritol 4-phosphate pathway and is an effective target of antimalarial drugs such as fosmidomycin. In the crystal structure, electron density for the flexible loop covering the active site was clearly observed, indicating the well ordered conformation of DXR upon substrate binding. On the other hand, no electron density was observed for the nicotinamide-ribose portion of NADPH and the position of Asp149 anchoring Mg(2+) was shifted by NADPH in the active site.

PubMed: 17554164
DOI: 10.1107/S1744309107024475

実験手法

X-RAY DIFFRACTION (2.2 Å)