1JVS

Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase; a target enzyme for antimalarial drugs

1JVS の概要

• エントリーDOI: 10.2210/pdb1jvs/pdb
• 分子名称: 1-deoxy-D-xylulose 5-phosphate reductoisomerase, SULFATE ION, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: reductoisomerase, nadph, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90402.95

構造登録者

Yajima, S.,Nonaka, T.,Kuzuyama, T.,Seto, H.,Ohsawa, K. (登録日: 2001-08-31, 公開日: 2002-10-09, 最終更新日: 2024-10-30)

主引用文献

Yajima, S.,Nonaka, T.,Kuzuyama, T.,Seto, H.,Ohsawa, K.
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with cofactors: implications of a flexible loop movement upon substrate binding.
J.Biochem., 131:313-317, 2002

PubMed Abstract: The key enzyme in the nonmevalonate pathway, 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), has been shown to be an effective target of antimalarial drugs. Here we report the crystal structure of DXR complexed with NADPH and a sulfate ion from Escherichia coli at 2.2 A resolution. The structure showed the presence of an extra domain, which is absent from other NADPH-dependent oxidoreductases, in addition to the conformation of catalytic residues and the substrate binding site. A flexible loop covering the substrate binding site plays an important role in the enzymatic reaction and the determination of substrate specificity.

PubMed: 11872159
DOI: 10.1093/oxfordjournals.jbchem.a003105

実験手法

X-RAY DIFFRACTION (2.2 Å)