HOLY PROTEINS .2. THE SOLUBLE LYTIC TRANSGLYCOSYLASE

Citation
Bw. Dijkstra et Amwh. Thunnissen, HOLY PROTEINS .2. THE SOLUBLE LYTIC TRANSGLYCOSYLASE, Current opinion in structural biology, 4(6), 1994, pp. 810-813
Citations number
15
Categorie Soggetti
Cell Biology",Biology
ISSN journal
0959440X
Volume
4
Issue
6
Year of publication
1994
Pages
810 - 813
Database
ISI
SICI code
0959-440X(1994)4:6<810:HP.TSL>2.0.ZU;2-U
Abstract
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.