E. Coli MurG: a paradigm for a superfamily of glycosyltransferases.
MurG is an essential bacterial glycosyltransferase that is involved in the biosynthesis of peptidoglycan. The enzyme is found in all organisms that synthesize peptidoglycan and is a target for the design of new antibiotics. A direct assay to study MurG was reported recently, followed shortly by the crystal structure of E. coli MurG. This first MurG structure, combined with sequence data on other glycosyltransferases, has revealed that MurG is a paradigm for a large family of metal ion-independent glycosyltransferases found in both eukaryotes and prokaryotes. A better understanding of MurG could lead to the development of new drugs to combat antibiotic resistant infections, and may also shed light on a broad class of glycosyltransferases.
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Chemistry Department, Princeton University, Princeton, NJ 08544, USA.
Gross
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Walker
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D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001425:Bacterial Outer Membrane Proteins; D001665:Binding Sites; D002473:Cell Wall / Q000187:drug effects / Q000378:metabolism; D015195:Drug Design; D024881:Drug Resistance, Bacterial; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology*; D008969:Molecular Sequence Data; D017351:N-Acetylglucosaminyltransferases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D010457:Peptidoglycan / Q000096:biosynthesis
D000900:Anti-Bacterial Agents; D001425:Bacterial Outer Membrane Proteins; D004791:Enzyme Inhibitors; D010457:Peptidoglycan; D017351:N-Acetylglucosaminyltransferases; C064057:UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase