Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase.

ABSTRACT: Enzymes in the prolyl oligopeptidase family possess unique structures and substrate specificities that are important for their biological activity and for potential biocatalytic applications. The crystal structures of Pyrococcus furiosus ( Pfu) prolyl oligopeptidase (POP) and the corresponding S477C mutant were determined to 1.9 and 2.2 Å resolution, respectively. The wild type enzyme crystallized in an open conformation, indicating that this state is readily accessible, and it contained bound chloride ions and a prolylproline ligand. These structures were used as starting points for molecular dynamics simulations of Pfu POP conformational dynamics. The simulations showed that large-scale domain opening and closing occurred spontaneously, providing facile substrate access to the active sit

SUBMITTER: Ellis-Guardiola K 

PROVIDER: S-EPMC6714975 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature