Enzymes involved in the metabolism of the bacterial cell wall peptidog
lycan are excellent targets for antibiotics. Penicillins and related b
eta-lactam antibiotics inhibit the enzymes that act on the peptide cro
ss-links of the peptidoglycan. The X-ray structure of the transglycosy
lase revealed a two-layered ring of alpha-helices in a right-handed su
perhelical arrangement with a separate catalytic domain on top, which
resembles the fold of goose-type lysozyme. Three sequence motifs were
found that characterize the catalytic and substrate-binding sites in t
he enzyme. These motifs are present in a broad family of muramidases a
nd chitinases.