PMID:11872159
| Citation |
Yajima, S, Nonaka, T, Kuzuyama, T, Seto, H and Ohsawa, K (2002) Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with cofactors: implications of a flexible loop movement upon substrate binding. J. Biochem. 131:313-7 |
|---|---|
| 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. |
| Links | |
| Keywords |
Aldose-Ketose Isomerases/chemistry; Aldose-Ketose Isomerases/metabolism; Binding Sites; Catalytic Domain/physiology; Crystallography; Erythritol/analogs & derivatives; Erythritol/chemistry; Erythritol/metabolism; Escherichia coli/enzymology; Models, Molecular; Multienzyme Complexes/chemistry; Multienzyme Complexes/metabolism; NADP/chemistry; NADP/metabolism; Oxidoreductases/chemistry; Oxidoreductases/metabolism; Pentosephosphates/chemistry; Pentosephosphates/metabolism; Protein Conformation; Protein Structure, Tertiary; Substrate Specificity; Sugar Phosphates/chemistry; Sugar Phosphates/metabolism |
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