1uek

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Revision as of 01:57, 21 November 2007

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spinqualitylabelsall models 1uek, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of 4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol kinase

Overview

The crystal structure of the enzyme 4-(cytidine, 5'-diphospho)-2-C-methyl-D-erythritol (CDP-ME) kinase from the, thermophilic bacterium Thermus thermophilus HB8 has been determined at, 1.7-A resolution. This enzyme catalyzes phosphorylation of the 2-hydroxyl, group of CDP-ME, the fourth step of the non-mevalonate pathway, which is, essential for isoprenoid biosynthesis in several pathogenic, microorganisms. Since this pathway is absent in humans, it is an important, target for the development of novel antimicrobial compounds. The structure, of the enzyme is similar to the structures of mevalonate kinase and, homoserine kinase, members of the GHMP superfamily. Lys8 and Asp125 are, active site residues in mevalonate kinase that also appear to play a, catalytic role in CDP-ME kinase. Both the mevalonate and the, non-mevalonate pathways therefore involve closely related kinases with, similar mechanisms. Assaying the enzyme showed that CDP-ME kinase will, phosphorylate CDP-ME but not 4-(uridine, 5'-diphospho)-2-C-methyl-D-erythritol, indicating the substrate pyrimidine, moiety is involved in important interactions with the enzyme.

About this Structure

1UEK is a Single protein structure of sequence from Thermus thermophilus. Active as 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, with EC number 2.7.1.148 Full crystallographic information is available from OCA.

Reference

Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis., Wada T, Kuzuyama T, Satoh S, Kuramitsu S, Yokoyama S, Unzai S, Tame JR, Park SY, J Biol Chem. 2003 Aug 8;278(32):30022-7. Epub 2003 May 27. PMID:12771135

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