Action of a minimal contractile bactericidal nanomachine.

Action of a minimal contractile bactericidal nanomachine.
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DOI:
10.1038/s41586-020-2186-z
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发表时间:
2020-04
期刊:
影响因子:
64.8
通讯作者:
Zhou ZH
Zhou ZH
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Ge P;Scholl D;Prokhorov NS;Avaylon J;Shneider MM;Browning C;Buth SA;Plattner M;Chakraborty U;Ding K;Leiman PG;Miller JF;Zhou ZH

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R-type bacteriocins are minimal contractile nanomachines that hold promise as precision antibiotics. Each bactericidal complex uses a collar to bridge a hollow tube with a contractile sheath loaded in a metastable state by a baseplate scaffold. 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 (DNA-containing) T4 bacteriophage. Here we report the atomic model of the complete R2 pyocin in its pre- and post-contraction states, each containing 384 subunits of 11 unique atomic models of 10 gene products. Comparison of these structures suggests the sequence of events during pyocin contraction: tail fibers trigger lateral dissociation of baseplate triplexes; the dissociation then initiates a cascade of events leading to sheath contraction; this contraction converts chemical energy into mechanical force to drive the iron-tipped tube across the bacterial cell surface, killing the bacterium.
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