Structures of Streptococcus pyogenes class A sortase in complex with substrate and product mimics provide key details of target recognition.

ABSTRACT: The cell wall is a critical extracellular barrier for bacteria and many other organisms. In bacteria, this structural layer consists of peptidoglycan, which maintains cell shape and structural integrity and provides a scaffold for displaying various protein factors. To attach proteins to the cell wall, Gram-positive bacteria utilize sortase enzymes, which are cysteine transpeptidases that recognize and cleave a specific sorting signal, followed by ligation of the sorting signal-containing protein to the peptidoglycan precursor lipid II (LII). This mechanism is the subject of considerable interest as a target for therapeutic intervention and as a tool for protein engineering, where sortases have enabled sortase-mediated ligation or sortagging strategies. Despite these uses, there remains an

SUBMITTER: Johnson DA 

PROVIDER: S-EPMC9520033 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature