2egh
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(New page: 200px<br /><applet load="2egh" size="350" color="white" frame="true" align="right" spinBox="true" caption="2egh, resolution 2.20Å" /> '''Crystal structure of...)
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Revision as of 12:48, 23 January 2008
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Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with a magnesium ion, NADPH and fosmidomycin
Overview
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.
About this Structure
2EGH is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as 1-deoxy-D-xylulose-5-phosphate reductoisomerase, with EC number 1.1.1.267 Full crystallographic information is available from OCA.
Reference
Structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in a quaternary complex with a magnesium ion, NADPH and the antimalarial drug fosmidomycin., Yajima S, Hara K, Iino D, Sasaki Y, Kuzuyama T, Ohsawa K, Seto H, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):466-70. Epub 2007 May 31. PMID:17554164
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