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Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei

Author

Listed:
  • Ryan J. Blackler

    (University of Victoria
    Zymeworks Inc.)

  • Arturo López-Guzmán

    (Universität für Bodenkultur Wien)

  • Fiona F. Hager

    (Universität für Bodenkultur Wien)

  • Bettina Janesch

    (Universität für Bodenkultur Wien)

  • Gudrun Martinz

    (Universität für Bodenkultur Wien)

  • Susannah M. L. Gagnon

    (University of Victoria)

  • Omid Haji-Ghassemi

    (University of Victoria
    University of British Columbia)

  • Paul Kosma

    (Universität für Bodenkultur Wien)

  • Paul Messner

    (Universität für Bodenkultur Wien)

  • Christina Schäffer

    (Universität für Bodenkultur Wien)

  • Stephen V. Evans

    (University of Victoria)

Abstract

Self-assembling protein surface (S-) layers are common cell envelope structures of prokaryotes and have critical roles from structural maintenance to virulence. S-layers of Gram-positive bacteria are often attached through the interaction of S-layer homology (SLH) domain trimers with peptidoglycan-linked secondary cell wall polymers (SCWPs). Here we present an in-depth characterization of this interaction, with co-crystal structures of the three consecutive SLH domains from the Paenibacillus alvei S-layer protein SpaA with defined SCWP ligands. The most highly conserved SLH domain residue SLH-Gly29 is shown to enable a peptide backbone flip essential for SCWP binding in both biophysical and cellular experiments. Furthermore, we find that a significant domain movement mediates binding by two different sites in the SLH domain trimer, which may allow anchoring readjustment to relieve S-layer strain caused by cell growth and division.

Suggested Citation

  • Ryan J. Blackler & Arturo López-Guzmán & Fiona F. Hager & Bettina Janesch & Gudrun Martinz & Susannah M. L. Gagnon & Omid Haji-Ghassemi & Paul Kosma & Paul Messner & Christina Schäffer & Stephen V. Ev, 2018. "Structural basis of cell wall anchoring by SLH domains in Paenibacillus alvei," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05471-3
    DOI: 10.1038/s41467-018-05471-3
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    Cited by:

    1. Adrià Sogues & Antonella Fioravanti & Wim Jonckheere & Els Pardon & Jan Steyaert & Han Remaut, 2023. "Structure and function of the EA1 surface layer of Bacillus anthracis," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Augustinas Silale & Yiling Zhu & Jerzy Witwinowski & Robert E. Smith & Kahlan E. Newman & Satya P. Bhamidimarri & Arnaud Baslé & Syma Khalid & Christophe Beloin & Simonetta Gribaldo & Bert Berg, 2023. "Dual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    3. Paola Lanzoni-Mangutchi & Oishik Banerji & Jason Wilson & Anna Barwinska-Sendra & Joseph A. Kirk & Filipa Vaz & Shauna O’Beirne & Arnaud Baslé & Kamel El Omari & Armin Wagner & Neil F. Fairweather & G, 2022. "Structure and assembly of the S-layer in C. difficile," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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