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 2.20&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17554164 17554164]
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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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):466-70. Epub 2007 May 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17554164 17554164]
[[Category: 1-deoxy-D-xylulose-5-phosphate reductoisomerase]]
[[Category: 1-deoxy-D-xylulose-5-phosphate reductoisomerase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: protein-inhibitor complex]]
[[Category: protein-inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:48:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:09:40 2008''

Revision as of 15:09, 21 February 2008


2egh, resolution 2.20Å

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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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):466-70. Epub 2007 May 31. PMID:17554164

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