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Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens

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  • Jaroslaw Sedzicki

    (Biozentrum, University of Basel)

  • Dongchun Ni

    (IPHYS, SB, EPFL, and Department of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne)

  • Frank Lehmann

    (Biozentrum, University of Basel)

  • Henning Stahlberg

    (IPHYS, SB, EPFL, and Department of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne)

  • Christoph Dehio

    (Biozentrum, University of Basel)

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.

Suggested Citation

  • Jaroslaw Sedzicki & Dongchun Ni & Frank Lehmann & Henning Stahlberg & Christoph Dehio, 2024. "Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45415-8
    DOI: 10.1038/s41467-024-45415-8
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    References listed on IDEAS

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    1. Thomas Jank & Stephanie Eckerle & Marcus Steinemann & Christoph Trillhaase & Marianne Schimpl & Sebastian Wiese & Daan M. F. van Aalten & Wolfgang Driever & Klaus Aktories, 2015. "Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere cell behaviour in zebrafish embryos," Nature Communications, Nature, vol. 6(1), pages 1-16, November.
    2. Laura Marr & Dipsikha Biswas & Leonard A. Daly & Christopher Browning & Sarah C. M. Vial & Daniel P. Maskell & Catherine Hudson & Jay A. Bertrand & John Pollard & Neil A. Ranson & Heena Khatter & Clai, 2022. "Mechanism of glycogen synthase inactivation and interaction with glycogenin," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    3. Jacob L. W. Morgan & Joanna Strumillo & Jochen Zimmer, 2013. "Crystallographic snapshot of cellulose synthesis and membrane translocation," Nature, Nature, vol. 493(7431), pages 181-186, January.
    4. Wei Chen & Peng Cao & Yuansheng Liu & Ailing Yu & Dong Wang & Lei Chen & Rajamanikandan Sundarraj & Zhiguang Yuchi & Yong Gong & Hans Merzendorfer & Qing Yang, 2022. "Structural basis for directional chitin biosynthesis," Nature, Nature, vol. 610(7931), pages 402-408, October.
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