Structural details of the glycosyltransferase step of peptidoglycan assembly

The importance of peptidoglycan in forming the basis of the bacterial cell wall has led to many studies investigating its synthesis. The step of cross-linkage via transpeptidation, and its inhibition by penicillins, has been extremely well characterized yet knowledge of the preceding glycosyltransfe...

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Bibliographic Details
Published in:Current opinion in structural biology 2008-10, Vol.18 (5), p.534-543
Main Authors: Lovering, Andrew L, Gretes, Michael, Strynadka, Natalie CJ
Format: Article
Language:English
Subjects:
Binding Sites
Catalytic Domain
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - pharmacology
Enzyme Stability
Models, Molecular
Muramidase - chemistry
Muramidase - metabolism
Peptidoglycan - biosynthesis
Peptidoglycan Glycosyltransferase - antagonists & inhibitors
Peptidoglycan Glycosyltransferase - chemistry
Peptidoglycan Glycosyltransferase - metabolism
Protein Conformation
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Summary:The importance of peptidoglycan in forming the basis of the bacterial cell wall has led to many studies investigating its synthesis. The step of cross-linkage via transpeptidation, and its inhibition by penicillins, has been extremely well characterized yet knowledge of the preceding glycosyltransfer reaction remained elusive until recently. The structures of two glycosyltransferase enzymes, catalyzing membrane-based polymerization of the lipid II monomer unit, have presented a means of elucidating the molecular details of this highly desirable antibiotic target. Evidence acquired before the publication of the structures is related here to these new findings, with particular emphasis on the recognition of substrates and inhibitors.
ISSN:0959-440X
1879-033X
DOI:10.1016/j.sbi.2008.07.002