7OFH

CryoEM structure of the outer membrane secretin pore pIV from the f1 filamentous bacteriophage.

Summary for 7OFH

• Entry DOI: 10.2210/pdb7ofh/pdb
• EMDB information: 12874
• Descriptor: Virion export protein, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE (2 entities in total)
• Functional Keywords: secretin outer membrane virion export, viral protein
• Biological source: Enterobacteria phage f1 (Bacteriophage f1)
• Total number of polymer chains: 15
• Total formula weight: 688311.92

Authors

Conners, R.,Gold, V.A.M. (deposition date: 2021-05-05, release date: 2021-11-03, Last modification date: 2024-07-10)

Primary citation

Conners, R.,McLaren, M.,Lapinska, U.,Sanders, K.,Stone, M.R.L.,Blaskovich, M.A.T.,Pagliara, S.,Daum, B.,Rakonjac, J.,Gold, V.A.M.
CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage.
Nat Commun, 12:6316-6316, 2021

PubMed Abstract: The Ff family of filamentous bacteriophages infect gram-negative bacteria, but do not cause lysis of their host cell. Instead, new virions are extruded via the phage-encoded pIV protein, which has homology with bacterial secretins. Here, we determine the structure of pIV from the f1 filamentous bacteriophage at 2.7 Å resolution by cryo-electron microscopy, the first near-atomic structure of a phage secretin. Fifteen f1 pIV subunits assemble to form a gated channel in the bacterial outer membrane, with associated soluble domains projecting into the periplasm. We model channel opening and propose a mechanism for phage egress. By single-cell microfluidics experiments, we demonstrate the potential for secretins such as pIV to be used as adjuvants to increase the uptake and efficacy of antibiotics in bacteria. Finally, we compare the f1 pIV structure to its homologues to reveal similarities and differences between phage and bacterial secretins.

PubMed: 34728631
DOI: 10.1038/s41467-021-26610-3

Experimental method

ELECTRON MICROSCOPY (2.7 Å)