ArticleNature communications2024
Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 11 citations in OpenAlex.
- Multi-omics reveals effects of several rumen bacteria on reproductive performance of sheep.Microbiome · 2026Article
- Cryo-EM Structures Reveal the Molecular Basis of Asymmetric Allosteric Activation by MMOB in the Hydroxylase of Soluble Methane Monooxygenase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Novel Lytic Bacteriophage PAT-A: Isolation, Characterization, Genome Analysis, and Biocontrol Potential AgainstMicroorganisms · 2026Article
- A β-1,2-glucan-associated glycoside hydrolase family 1 β-glucosidase from Streptomyces griseus.Protein science : a publication of the Protein Society · 2025Article
- Degree of polymerization and spatial distributions of acyclic and cyclic oligohexoses in soybean root nodules uncovered by MALDI and nanophotonic laser desorption ionization mass spectrometry.Materials today. Bio · 2025Article
- Acyltransferases that Modify Cell Surface Polymers Across the Membrane.Biochemistry · 2025Review
- Enzymes that catalyze cyclization of β-1,2-glucans.Applied microbiology and biotechnology · 2025Review
- Development of a scalable recombinant system for cyclic beta-1,2-glucans production.Microbial cell factories · 2024Article
- Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase.Applied microbiology and biotechnology · 2024Article
- Proteomics Exploration ofBioinformatics and biology insights · 2024Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The synthesis of complex sugars is a key aspect of microbial biology. Cyclic β-1,2-glucan (CβG) is a circular polysaccharide critical for host interactions of many bacteria, including major pathogens of humans (Brucella) and plants (Agrobacterium). CβG is produced by the cyclic glucan synthase (Cgs), a multi-domain membrane protein. So far, its structure as well as the mechanism underlining the synthesis have not been clarified. Here we use cryo-electron microscopy (cryo-EM) and functional approaches to study Cgs from A. tumefaciens. We determine the structure of this complex protein machinery and clarify key aspects of CβG synthesis, revealing a distinct mechanism that uses a tyrosine-linked oligosaccharide intermediate in cycles of polymerization and processing of the glucan chain. Our research opens possibilities for combating pathogens that rely on polysaccharide virulence factors and may lead to synthetic biology approaches for producing complex cyclic sugars.
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