Action of a minimal contractile bactericidal nanomachine.

ABSTRACT: 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 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 durin

SUBMITTER: Ge P 

PROVIDER: S-EPMC7513463 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature