1JVS
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase; a target enzyme for antimalarial drugs
Summary for 1JVS
| Entry DOI | 10.2210/pdb1jvs/pdb |
| Descriptor | 1-deoxy-D-xylulose 5-phosphate reductoisomerase, SULFATE ION, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | reductoisomerase, nadph, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 90402.95 |
| Authors | Yajima, S.,Nonaka, T.,Kuzuyama, T.,Seto, H.,Ohsawa, K. (deposition date: 2001-08-31, release date: 2002-10-09, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 11872159DOI: 10.1093/oxfordjournals.jbchem.a003105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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