ArticleJournal of bacteriology2009
Functional mapping of Brucella abortus cyclic beta-1,2-glucan synthase: identification of the protein domain required for cyclization.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Development of a scalable recombinant system for cyclic beta-1,2-glucans production.Microbial cell factories · 2024Article
- Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens.Nature communications · 2024Article
- Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase.Applied microbiology and biotechnology · 2024Article
- Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family.The Journal of biological chemistry · 2019Article
- Presence of Bacterial Virulence Gene Homologues in the dibenzo-p-dioxins degrading bacterium Sphingomonas wittichii.Bioinformation · 2016Article
- Interaction network and localization of Brucella abortus membrane proteins involved in the synthesis, transport, and succinylation of cyclic β-1,2-glucans.Journal of bacteriology · 2015Article
- Highly dynamic genomic loci drive the synthesis of two types of capsular or secreted polysaccharides within the Mycoplasma mycoides cluster.Applied and environmental microbiology · 2015Article
- In silico detection of virulence gene homologues in the human pathogen sphingomonas spp.Evolutionary bioinformatics online · 2014Article
- Study of free oligosaccharides derived from the bacterial N-glycosylation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 identification of the minimal region required for the catalysis of initiation and elongation reactions. In addition, we identified the Cgs region (residues 991 to 1544) as being the protein domain required for cyclization and demonstrated that upon cyclization and releasing of the CbetaG, one or more glucose residues remain attached to the protein intermediate that serves as a primer for the next round of CbetaG synthesis. Finally, our results indicate that the overall control of the degree of polymerization of CbetaG is the result of a balance between elongation, phosphorolysis, and cyclization reactions.
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