Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site.

ABSTRACT: Proteins with LytM (Peptidase_M23) domains are broadly distributed in bacteria and have been implicated in a variety of important processes, including cell division and cell-shape determination. Most LytM-like proteins that have been structurally and/or biochemically characterized are metallo-endopeptidases that cleave cross-links in the peptidoglycan (PG) cell wall matrix. Notable exceptions are the Escherichia coli cell division proteins EnvC and NlpD. These LytM factors are not hydrolases themselves, but instead serve as activators that stimulate PG cleavage by target enzymes called amidases to promote cell separation. Here we report the structure of the LytM domain from EnvC, the first structure of a LytM factor implicated in the regulation of PG hydrolysis. As expected, the fold is hi

SUBMITTER: Peters NT 

PROVIDER: S-EPMC3923381 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature