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7NSU

ColicinE9 intact translocation complex

Summary for 7NSU
Entry DOI10.2210/pdb7nsu/pdb
Related2IVZ 2YSU 3K19 5EW5
EMDB information12577
DescriptorOuter membrane protein F, Colicin-E9, Tol-Pal system protein TolB, ... (4 entities in total)
Functional Keywordsbacteriocin complex, import, membrane, membrane protein
Biological sourceEscherichia coli (strain K12)
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Total number of polymer chains6
Total formula weight285436.46
Authors
Webby, M.N.,Kleanthous, C.,Lukoyanova, N.,Housden, N.G. (deposition date: 2021-03-08, release date: 2021-08-11, Last modification date: 2024-11-06)
Primary citationFrancis, M.R.,Webby, M.N.,Housden, N.G.,Kaminska, R.,Elliston, E.,Chinthammit, B.,Lukoyanova, N.,Kleanthous, C.
Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.
Embo J., 40:e108610-e108610, 2021
Cited by
PubMed Abstract: Bacteria deploy weapons to kill their neighbours during competition for resources and to aid survival within microbiomes. Colicins were the first such antibacterial system identified, yet how these bacteriocins cross the outer membrane (OM) of Escherichia coli is unknown. Here, by solving the structures of translocation intermediates via cryo-EM and by imaging toxin import, we uncover the mechanism by which the Tol-dependent nuclease colicin E9 (ColE9) crosses the bacterial OM. We show that threading of ColE9's disordered N-terminal domain through two pores of the trimeric porin OmpF causes the colicin to disengage from its primary receptor, BtuB, and reorganises the translocon either side of the membrane. Subsequent import of ColE9 through the lumen of a single OmpF subunit is driven by the proton-motive force, which is delivered by the TolQ-TolR-TolA-TolB assembly. Our study answers longstanding questions, such as why OmpF is a better translocator than OmpC, and reconciles the mechanisms by which both Tol- and Ton-dependent bacteriocins cross the bacterial outer membrane.
PubMed: 34515361
DOI: 10.15252/embj.2021108610
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.7 Å)
Structure validation

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