Functional mapping of Brucella abortus cyclic beta-1,2-glucan synthase: identification of the protein domain required for cyclization.

ABSTRACT: Cyclic beta-1,2-glucans (CbetaG) are periplasmic homopolysaccharides that have been shown to play an important role in several symbiotic and pathogenic relationships. Cyclic beta-1,2-glucan synthase (Cgs), the enzyme responsible for the synthesis of CbetaG, is an integral membrane polyfunctional protein that catalyzes the four enzymatic activities (initiation, elongation, phosphorolysis, and cyclization) required for the synthesis of CbetaG. Recently, we have identified the glycosyltransferase and the beta-1,2-glucooligosaccharide phosphorylase domains of Brucella abortus Cgs. In this study, we performed large-scale linker-scanning mutagenesis to gain further insight into the functional domains of Cgs. This analysis allowed us to construct a functional map of the enzyme and led to the iden

SUBMITTER: Guidolin LS 

PROVIDER: S-EPMC2631987 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature