Action of a minimal contractile bactericidal nanomachine

Peng Ge, Dean Scholl, Nikolai S. Prokhorov, Jaycob Avaylon, Mikhail M. Shneider, Christopher Browning, Sergey A. Buth, Michel Plattner, Urmi Chakraborty, Ke Ding, Petr G. Leiman, Jeff F. Miller () and Z. Hong Zhou ()
Additional contact information
Peng Ge: University of California, Los Angeles (UCLA)
Dean Scholl: Pylum Biosciences
Nikolai S. Prokhorov: University of Texas Medical Branch, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics
Jaycob Avaylon: University of California, Los Angeles (UCLA)
Mikhail M. Shneider: Laboratory of Molecular Bioengineering
Christopher Browning: Vertex Pharmaceuticals (Europe) Ltd
Sergey A. Buth: University of Texas Medical Branch, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics
Michel Plattner: University of Texas Medical Branch, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics
Urmi Chakraborty: Pylum Biosciences
Ke Ding: University of California, Los Angeles (UCLA)
Petr G. Leiman: University of Texas Medical Branch, Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics
Jeff F. Miller: University of California, Los Angeles (UCLA)
Z. Hong Zhou: University of California, Los Angeles (UCLA)

Nature, 2020, vol. 580, issue 7805, 658-662

Abstract: Abstract R-type bacteriocins are minimal contractile nanomachines that hold promise as precision antibiotics1–4. Each bactericidal complex uses a collar to bridge a hollow tube with a contractile sheath loaded in a metastable state by a baseplate scaffold1,2. Fine-tuning of such nucleic acid-free protein machines for precision medicine calls for an atomic description of the entire complex and contraction mechanism, which is not available from baseplate structures of the (DNA-containing) T4 bacteriophage5. Here we report the atomic model of the complete R2 pyocin in its pre-contraction and post-contraction states, each containing 384 subunits of 11 unique atomic models of 10 gene products. Comparison of these structures suggests the following sequence of events during pyocin contraction: tail fibres trigger lateral dissociation of baseplate triplexes; the dissociation then initiates a cascade of events leading to sheath contraction; and this contraction converts chemical energy into mechanical force to drive the iron-tipped tube across the bacterial cell surface, killing the bacterium.

Date: 2020
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DOI: 10.1038/s41586-020-2186-z

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