2EGH
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with a magnesium ion, NADPH and fosmidomycin
Summary for 2EGH
Entry DOI | 10.2210/pdb2egh/pdb |
Descriptor | 1-deoxy-D-xylulose 5-phosphate reductoisomerase, MAGNESIUM ION, 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID, ... (5 entities in total) |
Functional Keywords | protein-inhibitor complex, oxidoreductase |
Biological source | Escherichia coli str. K12 substr. |
Total number of polymer chains | 2 |
Total formula weight | 94253.43 |
Authors | Yajima, S.,Hara, K.,Iino, D.,Sasaki, Y.,Kuzuyama, T.,Seto, H. (deposition date: 2007-03-01, release date: 2007-06-19, Last modification date: 2023-10-25) |
Primary citation | Yajima, S.,Hara, K.,Iino, D.,Sasaki, Y.,Kuzuyama, T.,Ohsawa, K.,Seto, H. Structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in a quaternary complex with a magnesium ion, NADPH and the antimalarial drug fosmidomycin Acta Crystallogr.,Sect.F, 63:466-470, 2007 Cited by PubMed Abstract: The crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) from Escherichia coli complexed with Mg(2+), NADPH and fosmidomycin was solved at 2.2 A resolution. DXR is the key enzyme in the 2-C-methyl-D-erythritol 4-phosphate pathway and is an effective target of antimalarial drugs such as fosmidomycin. In the crystal structure, electron density for the flexible loop covering the active site was clearly observed, indicating the well ordered conformation of DXR upon substrate binding. On the other hand, no electron density was observed for the nicotinamide-ribose portion of NADPH and the position of Asp149 anchoring Mg(2+) was shifted by NADPH in the active site. PubMed: 17554164DOI: 10.1107/S1744309107024475 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
