A Putative Interaction between the Transmembrane Domains of <i>Streptococcus pyogenes</i> Sortase A and Its Endogenous Substrate M Protein Revealed by Molecular Dynamics Simulations.

ABSTRACT: Sortase enzymes are cysteine transpeptidases at the cell surface of Gram-positive bacteria. Localized to distinct foci on the cell membrane, class A sortases (SrtAs) recognize a cell wall sorting signal (CWSS), and, following cleavage at this specific binding motif, target proteins are ligated to precursors of the growing peptidoglycan layer. This activity of SrtA enzymes is utilized extensively in sortase-mediated ligation (SML) strategies for a variety of protein engineering applications. Typically, engineered variants of SrtA are used for SML experiments, considering the relatively low catalytic efficiency of this enzyme. Understandably, most biochemical studies are conducted with the isolated catalytic domain of SrtA enzymes from various bacteria, and the stereochemistry of the endogen

SUBMITTER: Avery NG 

PROVIDER: S-EPMC12746448 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature