1i52
From Proteopedia
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CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS
Overview
The YgbP protein of Escherichia coli encodes the enzyme, 4-diphosphocytidyl-2-C-methylerythritol (CDP-ME) synthetase, a member of, the cytidyltransferase family of enzymes. CDP-ME is an intermediate in the, mevalonate-independent pathway for isoprenoid biosynthesis in a number of, prokaryotic organisms, algae, the plant plastids and the malaria parasite., Because vertebrates synthesize isoprenoid precursors using a mevalonate, pathway, CDP-ME synthetase and other enzymes of the mevalonate-independent, pathway for isoprenoid production represent attractive targets for the, structure-based design of selective antibacterial, herbicidal and, antimalarial drugs. The high-resolution structures of E. coli CDP-ME, synthetase in the apo form and complexed with both CTP-Mg2+ and, CDP-ME-Mg2+ reveal the stereochemical principles underlying both substrate, and product recognition as well as catalysis in CDP-ME synthetase., Moreover, these complexes represent the first experimental structures for, any cytidyltransferase with both substrates and products bound.
About this Structure
1I52 is a Single protein structure of sequence from Escherichia coli with CA, MG and CTP as ligands. Full crystallographic information is available from OCA.
Reference
Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis., Richard SB, Bowman ME, Kwiatkowski W, Kang I, Chow C, Lillo AM, Cane DE, Noel JP, Nat Struct Biol. 2001 Jul;8(7):641-8. PMID:11427897
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