Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan.

ABSTRACT: Endolysins, the cell wall lytic enzymes encoded by bacteriophages to release the phage progeny, are among the top alternatives to fight against multiresistant pathogenic bacteria; one of the current biggest challenges to global health. Their narrow range of susceptible bacteria relies, primarily, on targeting specific cell-wall receptors through specialized modules. The cell wall-binding domain of Cpl-7 endolysin, made of three CW_7 repeats, accounts for its extended-range of substrates. Using as model system the cell wall-binding domain of Cpl-7, here we describe the molecular basis for the bacterial cell wall recognition by the CW_7 motif, which is widely represented in sequences of cell wall hydrolases. We report the crystal and solution structure of the full-length domain, identify N-a

SUBMITTER: Bustamante N 

PROVIDER: S-EPMC5705596 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature