Structure and cell wall cleavage by modular lytic transglycosylase MltC of Escherichia coli.

ABSTRACT: The lytic transglycosylases are essential bacterial enzymes that catalyze the nonhydrolytic cleavage of the glycan strands of the bacterial cell wall. We describe here the structural and catalytic properties of MltC, one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The 2.3 Å resolution X-ray structure of a soluble construct of MltC shows a unique, compared to known lytic transglycosylase structures, two-domain structure characterized by an expansive active site of 53 Å length extending through an interface between the domains. The structures of three complexes of MltC with cell wall analogues suggest the positioning of the peptidoglycan in the active site both as a substrate and as a product. One complex is suggested to correspon

SUBMITTER: Artola-Recolons C 

PROVIDER: S-EPMC4168783 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature