A Buried Water Network Modulates the Activity of the Escherichia coli Disulphide Catalyst DsbA.

ABSTRACT: The formation of disulphide bonds is an essential step in the folding of many proteins that enter the secretory pathway; therefore, it is not surprising that eukaryotic and prokaryotic organisms have dedicated enzymatic systems to catalyse this process. In bacteria, one such enzyme is disulphide bond-forming protein A (DsbA), a thioredoxin-like thiol oxidase that catalyses the oxidative folding of proteins required for virulence and fitness. A large body of work on DsbA proteins, particularly Escherichia coli DsbA (EcDsbA), has demonstrated the key role that the Cys³⁰-XX-Cys³³ catalytic motif and its unique redox properties play in the thiol oxidase activity of this enzyme. Using mutational and functional analyses, here we identify that a set of charged residue

SUBMITTER: Wang G 

PROVIDER: S-EPMC9952396 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature