Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with cofactors: Implications of a flexible loop movement upon substrate binding

被引：91

作者：

Yajima, S ^{[1
]}

Nonaka, T

Kuzuyama, T

Seto, H

Ohsawa, K

机构：

[1] Tokyo Univ Agr, Dept Biosci, Setagaya Ku, Tokyo 1568502, Japan

[2] Nagaoka Univ Technol, Dept Bioengn, Niigata 9402188, Japan

[3] Univ Tokyo, Inst Mol & Cellular Biosci, Bunkyo Ku, Tokyo 1130032, Japan

来源：

JOURNAL OF BIOCHEMISTRY | 2002年 / 131卷 / 03期

关键词：

crystal structure; Escherichia coli; MAD; nonmevalonate pathway; reductoisomerase;

D O I：

10.1093/oxfordjournals.jbchem.a003105

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：313 / 317

页数：5

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