1INI

CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHETASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS, COMPLEXED WITH CDP-ME AND MG2+

Summary for 1INI

• Entry DOI: 10.2210/pdb1ini/pdb
• Related: 1I52 1INJ
• Descriptor: 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL SYNTHETASE, MAGNESIUM ION, 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL, ... (4 entities in total)
• Functional Keywords: ygbp, cytidylyltransferase, deoxyxylulose-5-phosphate pathway (dxp), isoprenoid biosynthesis, cdpme, mg, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 26317.88

Authors

Richard, S.B.,Bowman, M.E.,Kwiatkowski, W.,Kang, I.,Chow, C.,Lillo, A.,Cane, D.E.,Noel, J.P. (deposition date: 2001-05-14, release date: 2001-11-14, Last modification date: 2023-08-16)

Primary citation

Richard, S.B.,Bowman, M.E.,Kwiatkowski, W.,Kang, I.,Chow, C.,Lillo, A.M.,Cane, D.E.,Noel, J.P.
Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis.
Nat.Struct.Biol., 8:641-648, 2001

PubMed Abstract: 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.

PubMed: 11427897
DOI: 10.1038/89691

Experimental method

X-RAY DIFFRACTION (1.82 Å)