Bacterial proteins of the Dsb (disulfide bond) system catalyze the formation of disulfide bridges, a post-translational modification of extra-cytoplasmic proteins, which leads to stabilization of their tertiary and quaternary structures and often influences their activity. DsbA – Escherichia coli monomeric oxidoreductase is the best studied protein involved in this process. Recent rapid advances in global analysis of bacteria have thrown light on the enormous diversity among bacterial Dsb systems. The set of Dsb proteins involved in the oxidative pathway, varies, depending on the microorganism. In this article we have focused on characterization of structural and phylogenetic groups of monomeric DsbAs. This review discuss their physicochemical features and interactions with redox partners as well as with substrate proteins. The last part of the review concentrates on dimeric oxidoreductases responsible for disulfide generation. Many virulence factors are the substrates of the Dsb proteins. Thus unraveling the machinery that introduces disulfide bonds and expanding knowledge about Dsb protein structures and their activities may facilitate the discovery of an effective anti-bacterial drugs.
1. Introduction. 2. Escherichia coli Dsb system. 2.1. Characteristic of the E. coli thiol oxidoreductase – DsbA. 2.2. Izomerization / reduction pathway proteins. 3. Classification of the monomeric DsbAs. 3.1. Physicochemical features of different classes of DsbAs. 4. DsbA interactions with redox partner and substrates. 4.1. DsbA interactions with redox partner. 4.2. DsbA interactions with substrates. 5. Dimeric Dsb proteins with oxidative activity. 6. Conclusions. 7. References
