Applications of the class II lanthipeptide protease LicP for sequence-specific, traceless peptide bond cleavage.

ABSTRACT: The final step of lanthipeptide biosynthesis involves the removal of leader peptides by dedicated proteases. In vitro characterization of LicP, a class II LanP protease involved in the biosynthesis of the lantibiotic lichenicidin, revealed a self-cleavage step that removes 100 amino acids from the N-terminus. The 2.35 Å resolution crystal structure provides insights into the active site geometry and substrate specificity, and unveiled an unusual calcium-independent maturation mechanism of a subtilisin family member. LicP processes LicA2 peptides with or without post-translational modifications, but dehydrated and cyclized LicA2 is favored. Investigation of its substrate specificity demonstrated that LicP can serve as an efficient sequence-specific traceless protease and may have gre

SUBMITTER: Tang W 

PROVIDER: S-EPMC6054071 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature