Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with cofactors: Implications of a flexible loop movement upon substrate binding
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with cofactors: Implications of a flexible loop movement upon substrate binding
复制标题
DOI：
10.1093/oxfordjournals.jbchem.a003105
复制
发表时间：
2002-03-01
影响因子：
2.7
通讯作者：
Ohsawa, K
中科院分区：
文献类型：
--
作者：
Yajima, S;Nonaka, T;Ohsawa, K
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.
