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Molecular architecture of the PBP2–MreC core bacterial cell wall synthesis complex

Author

Listed:
  • Carlos Contreras-Martel

    (Bacterial Pathogenesis Group)

  • Alexandre Martins

    (Bacterial Pathogenesis Group)

  • Chantal Ecobichon

    (Unit of Biology and Genetics of the Bacterial Cell Wall
    Groupe Avenir)

  • Daniel Maragno Trindade

    (CNPEM, Campinas)

  • Pierre-Jean Matteï

    (Bacterial Pathogenesis Group)

  • Samia Hicham

    (Unit of Biology and Genetics of the Bacterial Cell Wall
    Groupe Avenir)

  • Pierre Hardouin

    (Bacterial Pathogenesis Group)

  • Meriem El Ghachi

    (Unit of Biology and Genetics of the Bacterial Cell Wall
    Groupe Avenir)

  • Ivo G. Boneca

    (Unit of Biology and Genetics of the Bacterial Cell Wall
    Groupe Avenir)

  • Andréa Dessen

    (Bacterial Pathogenesis Group
    CNPEM, Campinas)

Abstract

Bacterial cell wall biosynthesis is an essential process that requires the coordinated activity of peptidoglycan biosynthesis enzymes within multi-protein complexes involved in cell division (the “divisome”) and lateral wall growth (the “elongasome”). MreC is a structural protein that serves as a platform during wall elongation, scaffolding other essential peptidoglycan biosynthesis macromolecules, such as penicillin-binding proteins. Despite the importance of these multi-partite complexes, details of their architecture have remained elusive due to the transitory nature of their interactions. Here, we present the crystal structures of the soluble PBP2:MreC core elongasome complex from Helicobacter pylori, and of uncomplexed PBP2. PBP2 recognizes the two-winged MreC molecule upon opening of its N-terminal region, revealing a hydrophobic zipper that serves as binding platform. The PBP2:MreC interface is essential both for protein recognition in vitro and maintenance of bacterial shape and growth. This work allows visualization as to how peptidoglycan machinery proteins are scaffolded, revealing interaction regions that could be targeted by tailored inhibitors.

Suggested Citation

  • Carlos Contreras-Martel & Alexandre Martins & Chantal Ecobichon & Daniel Maragno Trindade & Pierre-Jean Matteï & Samia Hicham & Pierre Hardouin & Meriem El Ghachi & Ivo G. Boneca & Andréa Dessen, 2017. "Molecular architecture of the PBP2–MreC core bacterial cell wall synthesis complex," Nature Communications, Nature, vol. 8(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00783-2
    DOI: 10.1038/s41467-017-00783-2
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    Cited by:

    1. Irina Shlosman & Elayne M. Fivenson & Morgan S. A. Gilman & Tyler A. Sisley & Suzanne Walker & Thomas G. Bernhardt & Andrew C. Kruse & Joseph J. Loparo, 2023. "Allosteric activation of cell wall synthesis during bacterial growth," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Michael D. Sacco & Shaohui Wang & Swamy R. Adapa & Xiujun Zhang & Eric M. Lewandowski & Maura V. Gongora & Dimitra Keramisanou & Zachary D. Atlas & Julia A. Townsend & Jean R. Gatdula & Ryan T. Morgan, 2022. "A unique class of Zn2+-binding serine-based PBPs underlies cephalosporin resistance and sporogenesis in Clostridioides difficile," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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