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9FS5

Cryo-EM structure of the decameric TraT surface exclusion lipoprotein from Escherichia coli (F plasmid)

Summary for 9FS5
Entry DOI10.2210/pdb9fs5/pdb
EMDB information50723
DescriptorTraT complement resistance protein (1 entity in total)
Functional Keywordssurface exclusion, decamer, diacylglycerol (dag) modification, membrane protein
Biological sourceEscherichia coli
Total number of polymer chains10
Total formula weight239790.94
Authors
Seddon, C.,Beis, K. (deposition date: 2024-06-20, release date: 2024-12-11, Last modification date: 2025-06-11)
Primary citationSeddon, C.,David, S.,Wong, J.L.C.,Ishimoto, N.,He, S.,Bradshaw, J.,Low, W.W.,Frankel, G.,Beis, K.
Cryo-EM structure and evolutionary history of the conjugation surface exclusion protein TraT.
Nat Commun, 16:659-659, 2025
Cited by
PubMed Abstract: Conjugation plays a major role in dissemination of antimicrobial resistance genes. Following transfer of IncF-like plasmids, recipients become refractory to a second wave of conjugation with the same plasmid via entry (TraS) and surface (TraT) exclusion mechanisms. Here, we show that TraT from the pKpQIL and F plasmids (TraT and TraT) exhibits plasmid surface exclusion specificity. The cryo-EM structures of TraT and TraT reveal that they oligomerise into decameric champagne bottle cork-like structures, which are anchored to the outer membrane via a diacylglycerol and palmitic acid modified α-helical barrel domain. Unexpectedly, we identify chromosomal TraT homologues from multiple Gram-negative phyla which form numerous divergent lineages in a phylogenetic tree of TraT sequences. Plasmid-associated TraT sequences are found in multiple distinct lineages, including two separate clades incorporating TraT from Enterobacteriaceae IncF/F-like and Legionellaceae F-like plasmids. These findings suggest that different plasmid backbones have acquired and co-opted TraT on independent occasions.
PubMed: 39809778
DOI: 10.1038/s41467-025-55834-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.66 Å)
Structure validation

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