Architecturally complex O-glycopeptidases are customized for mucin recognition and hydrolysis.

ABSTRACT: A challenge faced by peptidases is the recognition of highly diverse substrates. A feature of some peptidase families is the capacity to specifically use post-translationally added glycans present on their protein substrates as a recognition determinant. This is ultimately critical to enabling peptide bond hydrolysis. This class of enzyme is also frequently large and architecturally sophisticated. However, the molecular details underpinning glycan recognition by these O-glycopeptidases, the importance of these interactions, and the functional roles of their ancillary domains remain unclear. Here, using the Clostridium perfringens ZmpA, ZmpB, and ZmpC M60 peptidases as model proteins, we provide structural and functional insight into how these intricate proteins recognize glyc

SUBMITTER: Pluvinage B 

PROVIDER: S-EPMC7958395 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature