PMID:10545329

Citation	van Asselt, EJ, Dijkstra, AJ, Kalk, KH, Takacs, B, Keck, W and Dijkstra, BW (1999) Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand. Structure 7:1167-80
Abstract	Lytic transglycosylases are bacterial muramidases that catalyse the cleavage of the beta- 1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue. These muramidases play an important role in the metabolism of the bacterial cell wall and might therefore be potential targets for the rational design of antibacterial drugs. One of the lytic transglycosylases is Slt35, a naturally occurring soluble fragment of the outer membrane bound lytic transglycosylase B (MltB) from Escherichia coli.
Links	PubMed
Keywords	Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Binding Sites; Calcium/metabolism; Catalytic Domain; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Glycoside Hydrolases; Glycosyltransferases/chemistry; Glycosyltransferases/genetics; Glycosyltransferases/metabolism; Models, Molecular; Molecular Sequence Data; Muramidase/chemistry; Peptidoglycan/metabolism; Protein Conformation; Protein Structure, Secondary; Sequence Homology, Amino Acid
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