Open AccessAction of a minimal contractile bactericidal nanomachine
Author(s) -
Peng Ge,
Dean Scholl,
Nikolai S. Prokhorov,
Jaycob Avaylon,
Mikhail M. Shneider,
C. H. Browning,
S.A. Buth,
M. Plattner,
Urmi Chakraborty,
Ke Ding,
P.G. Leiman,
Jeff F. Miller,
Z. Hong Zhou
Publication year - 2020
Publication title -
nature
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 15.993
H-Index - 1226
eISSN - 1476-4687
pISSN - 0028-0836
DOI - 10.1038/s41586-020-2186-z
Subject(s) - contraction (grammar) , biophysics , dna , bacteriocin , chemistry , crystallography , biology , bacteria , biochemistry , genetics , endocrinology
R-type bacteriocins are minimal contractile nanomachines that hold promise as precision antibiotics 1-4 . Each bactericidal complex uses a collar to bridge a hollow tube with a contractile sheath loaded in a metastable state by a baseplate scaffold 1,2 . 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 bacteriophage 5 . 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.