6PYT

CryoEM Structure of Pyocin R2 - precontracted - trunk

Summary for 6PYT

• Entry DOI: 10.2210/pdb6pyt/pdb
• EMDB information: 20526
• Descriptor: Pyocin tube PA0623, Pyocin sheath PA0622 (2 entities in total)
• Functional Keywords: bacteriocin, pyocin, helix, antimicrobial protein
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1); More
• Total number of polymer chains: 24
• Total formula weight: 710456.21

Authors

Ge, P.,Avaylon, J.,Scholl, D.,Shneider, M.M.,Browning, C.,Buth, S.A.,Plattner, M.,Ding, K.,Leiman, P.G.,Miller, J.F.,Zhou, Z.H. (deposition date: 2019-07-30, release date: 2020-04-15, Last modification date: 2024-03-20)

Primary citation

Ge, P.,Scholl, D.,Prokhorov, N.S.,Avaylon, J.,Shneider, M.M.,Browning, C.,Buth, S.A.,Plattner, M.,Chakraborty, U.,Ding, K.,Leiman, P.G.,Miller, J.F.,Zhou, Z.H.
Action of a minimal contractile bactericidal nanomachine.
Nature, 580:658-662, 2020

PubMed Abstract: 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 the (DNA-containing) T4 bacteriophage. 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.

PubMed: 32350467
DOI: 10.1038/s41586-020-2186-z

Experimental method

ELECTRON MICROSCOPY (2.9 Å)