5CES

C-terminal domain of the R-type pyocin baseplate protein PA0618

Summary for 5CES

• Entry DOI: 10.2210/pdb5ces/pdb
• Descriptor: PA0618 (2 entities in total)
• Functional Keywords: gpj, gp6, structural protein
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 2
• Total formula weight: 22603.31

Authors

Plattner, M.,Buth, S.A.,Shneider, M.M.,Leiman, P.G. (deposition date: 2015-07-07, release date: 2016-07-27, Last modification date: 2024-05-08)

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

X-RAY DIFFRACTION (2.102 Å)