期刊
JOURNAL OF BIOCHEMISTRY
卷 131, 期 3, 页码 313-317出版社
OXFORD UNIV PRESS
DOI: 10.1093/oxfordjournals.jbchem.a003105
关键词
crystal structure; Escherichia coli; MAD; nonmevalonate pathway; reductoisomerase
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.
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