2oqo
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Crystal structure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis
OverviewOverview
Peptidoglycan is an essential polymer that forms a protective shell around, bacterial cell membranes. Peptidoglycan biosynthesis is the target of many, clinically used antibiotics, including the beta-lactams, imipenems, cephalosporins, and glycopeptides. Resistance to these and other, antibiotics has prompted interest in an atomic-level understanding of the, enzymes that make peptidoglycan. Representative structures have been, reported for most of the enzymes in the pathway. Until now, however, there, have been no structures of any peptidoglycan glycosyltransferases (also, known as transglycosylases), which catalyze formation of the carbohydrate, chains of peptidoglycan from disaccharide subunits on the bacterial cell, surface. We report here the 2.1-A crystal structure of the peptidoglycan, glycosyltransferase (PGT) domain of Aquifex aeolicus PBP1A. The structure, has a different fold from all other glycosyltransferase structures, reported to date, but it bears some resemblance to lambda-lysozyme, an, enzyme that degrades the carbohydrate chains of peptidoglycan. An analysis, of the structure, combined with biochemical information showing that these, enzymes are processive, suggests a model for glycan chain polymerization.
About this StructureAbout this Structure
2OQO is a Single protein structure of sequence from Aquifex aeolicus with EPE and CPS as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis., Yuan Y, Barrett D, Zhang Y, Kahne D, Sliz P, Walker S, Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5348-53. Epub 2007 Mar 8. PMID:17360321
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