title: 'Holy' proteins. II: The soluble lytic transglycosylase.
abstract: Enzymes involved in the metabolism of the bacterial cell wall peptidoglycan are excellent targets for antibiotics. Penicillins and related beta-lactam antibiotics inhibit the enzymes that act on the peptide cross-links of the peptidoglycan. The X-ray structure of the transglycosylase revealed a two-layered ring of alpha-helices in a right-handed superhelical 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 the enzyme. These motifs are present in a broad family of muramidases and chitinases.
authors.affiliation: Laboratory of Biophysical Chemistry, University of Groningen, The Netherlands.
authors.forename: B W
authors.initials: BW
authors.lastname: Dijkstra
authors.forename: A M
authors.initials: AM
authors.lastname: Thunnissen
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D029968:Escherichia coli Proteins; D006026:Glycoside Hydrolases; D016695:Glycosyltransferases / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D016695:Glycosyltransferases; C021815:murein transglycosylase; D006026:Glycoside Hydrolases; C085428:slt protein, E coli