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Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter

Author

Listed:
  • Nicholas Spellmon

    (University of Virginia School of Medicine
    University of Virginia School of Medicine)

  • Artur Muszyński

    (University of Georgia)

  • Ireneusz Górniak

    (University of Virginia School of Medicine
    University of Virginia School of Medicine)

  • Jiri Vlach

    (University of Georgia)

  • David Hahn

    (University of Georgia)

  • Parastoo Azadi

    (University of Georgia)

  • Jochen Zimmer

    (University of Virginia School of Medicine
    University of Virginia School of Medicine)

Abstract

O antigens are ubiquitous protective extensions of lipopolysaccharides in the extracellular leaflet of the Gram-negative outer membrane. Following biosynthesis in the cytosol, the lipid-linked polysaccharide is transported to the periplasm by the WzmWzt ABC transporter. Often, O antigen secretion requires the chemical modification of its elongating terminus, which the transporter recognizes via a carbohydrate-binding domain (CBD). Here, using components from A. aeolicus, we identify the O antigen structure with methylated mannose or rhamnose as its cap. Crystal and cryo electron microscopy structures reveal how WzmWzt recognizes this cap between its carbohydrate and nucleotide-binding domains in a nucleotide-free state. ATP binding induces drastic conformational changes of its CBD, terminating interactions with the O antigen. ATPase assays and site directed mutagenesis reveal reduced hydrolytic activity upon O antigen binding, likely to facilitate polymer loading into the ABC transporter. Our results elucidate critical steps in the recognition and translocation of polysaccharides by ABC transporters.

Suggested Citation

  • Nicholas Spellmon & Artur Muszyński & Ireneusz Górniak & Jiri Vlach & David Hahn & Parastoo Azadi & Jochen Zimmer, 2022. "Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32597-2
    DOI: 10.1038/s41467-022-32597-2
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    References listed on IDEAS

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    1. Christopher A. Caffalette & Robin A. Corey & Mark S. P. Sansom & Phillip J. Stansfeld & Jochen Zimmer, 2019. "A lipid gating mechanism for the channel-forming O antigen ABC transporter," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    2. Yunchen Bi & Evan Mann & Chris Whitfield & Jochen Zimmer, 2018. "Architecture of a channel-forming O-antigen polysaccharide ABC transporter," Nature, Nature, vol. 553(7688), pages 361-365, January.
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    Cited by:

    1. Lorena Ilcu & Lukas Denkhaus & Anton Brausemann & Lin Zhang & Oliver Einsle, 2023. "Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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