Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase.

ABSTRACT: The assembly and anchorage of various pathogenic proteins on the surface of Gram-positive bacteria is mediated by the sortase family of enzymes. These cysteine transpeptidases catalyze a unique sorting signal motif located at the C-terminus of their target substrate and promote the covalent attachment of these proteins onto an amino nucleophile located on another protein or on the bacterial cell wall. Each of the six distinct classes of sortases displays a unique biological role, with sequential activation of multiple sortases often observed in many Gram-positive bacteria to decorate their peptidoglycans. Less is known about the members of the class D family of sortases (SrtD), but they have a suggested role in spore formation in an oxygen-limiting environment. Here, the crystal structure

SUBMITTER: Suryadinata R 

PROVIDER: S-EPMC4498605 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature