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Structure of the type VI secretion system TssK–TssF–TssG baseplate subcomplex revealed by cryo-electron microscopy

Author

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  • Young-Jun Park

    (University of Washington)

  • Kaitlyn D. Lacourse

    (University of Washington)

  • Christian Cambillau

    (Architecture et Fonction des Macromolecules Biologiques, Aix-Marseille Universite, CNRS)

  • Frank DiMaio

    (University of Washington)

  • Joseph D. Mougous

    (University of Washington
    University of Washington)

  • David Veesler

    (University of Washington)

Abstract

Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the baseplate remain unknown. Here, we report the 3.7 Å resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS baseplate architecture.

Suggested Citation

  • Young-Jun Park & Kaitlyn D. Lacourse & Christian Cambillau & Frank DiMaio & Joseph D. Mougous & David Veesler, 2018. "Structure of the type VI secretion system TssK–TssF–TssG baseplate subcomplex revealed by cryo-electron microscopy," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07796-5
    DOI: 10.1038/s41467-018-07796-5
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