Structural and biochemical analyses of selectivity determinants in chimeric Streptococcus Class A sortase enzymes.

ABSTRACT: Sequence variation in related proteins is an important characteristic that modulates activity and selectivity. An example of a protein family with a large degree of sequence variation is that of bacterial sortases, which are cysteine transpeptidases on the surface of gram-positive bacteria. Class A sortases are responsible for attachment of diverse proteins to the cell wall to facilitate environmental adaption and interaction. These enzymes are also used in protein engineering applications for sortase-mediated ligations (SML) or sortagging of protein targets. We previously investigated SrtA from Streptococcus pneumoniae, identifying a number of putative β7-β8 loop-mediated interactions that affected in vitro enzyme function. We identified residues that contributed to the ability of S. pneu

SUBMITTER: Gao M 

PROVIDER: S-EPMC8862441 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature