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Structure of the conjugation surface exclusion protein TraT
by
Lundgren, Camilla A. K.
, El Sayyed, Hafez
, Chen, Nicolas
, Berks, Ben C.
, Bukys, Alfredas
, Kapanidis, Achillefs N.
, Deme, Justin C.
, Lea, Susan M.
in
101/28
/ 14/35
/ 631/326/41/2180
/ 631/326/41/2536
/ Antimicrobial resistance
/ Bacterial Outer Membrane Proteins - chemistry
/ Bacterial Outer Membrane Proteins - genetics
/ Bacterial Outer Membrane Proteins - metabolism
/ Biomedical and Life Sciences
/ Conjugation
/ Conjugation, Genetic
/ Cryoelectron Microscopy
/ Data collection
/ Detergents
/ Escherichia coli
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Escherichia coli Proteins - ultrastructure
/ Gene transfer
/ Life Sciences
/ Ligands
/ Lipids
/ Models, Molecular
/ Mutagenesis
/ Outer membrane proteins
/ Plasmids
/ Protein Conformation
/ Proteins
2025
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Structure of the conjugation surface exclusion protein TraT
by
Lundgren, Camilla A. K.
, El Sayyed, Hafez
, Chen, Nicolas
, Berks, Ben C.
, Bukys, Alfredas
, Kapanidis, Achillefs N.
, Deme, Justin C.
, Lea, Susan M.
in
101/28
/ 14/35
/ 631/326/41/2180
/ 631/326/41/2536
/ Antimicrobial resistance
/ Bacterial Outer Membrane Proteins - chemistry
/ Bacterial Outer Membrane Proteins - genetics
/ Bacterial Outer Membrane Proteins - metabolism
/ Biomedical and Life Sciences
/ Conjugation
/ Conjugation, Genetic
/ Cryoelectron Microscopy
/ Data collection
/ Detergents
/ Escherichia coli
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Escherichia coli Proteins - ultrastructure
/ Gene transfer
/ Life Sciences
/ Ligands
/ Lipids
/ Models, Molecular
/ Mutagenesis
/ Outer membrane proteins
/ Plasmids
/ Protein Conformation
/ Proteins
2025
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Structure of the conjugation surface exclusion protein TraT
by
Lundgren, Camilla A. K.
, El Sayyed, Hafez
, Chen, Nicolas
, Berks, Ben C.
, Bukys, Alfredas
, Kapanidis, Achillefs N.
, Deme, Justin C.
, Lea, Susan M.
in
101/28
/ 14/35
/ 631/326/41/2180
/ 631/326/41/2536
/ Antimicrobial resistance
/ Bacterial Outer Membrane Proteins - chemistry
/ Bacterial Outer Membrane Proteins - genetics
/ Bacterial Outer Membrane Proteins - metabolism
/ Biomedical and Life Sciences
/ Conjugation
/ Conjugation, Genetic
/ Cryoelectron Microscopy
/ Data collection
/ Detergents
/ Escherichia coli
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Escherichia coli Proteins - ultrastructure
/ Gene transfer
/ Life Sciences
/ Ligands
/ Lipids
/ Models, Molecular
/ Mutagenesis
/ Outer membrane proteins
/ Plasmids
/ Protein Conformation
/ Proteins
2025
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Structure of the conjugation surface exclusion protein TraT
Journal Article
Structure of the conjugation surface exclusion protein TraT
2025
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Overview
Conjugal transfer of plasmids between bacteria is a major route for the spread of antimicrobial resistance. Many conjugative plasmids encode exclusion systems that inhibit redundant conjugation. In incompatibility group F (IncF) plasmids surface exclusion is mediated by the outer membrane protein TraT. Here we report the cryoEM structure of the TraT exclusion protein complex from the canonical F plasmid of
Escherichia coli
. TraT is a hollow homodecamer shaped like a chef’s hat. In contrast to most outer membrane proteins, TraT spans the outer membrane using transmembrane α-helices. We develop a microscopy-based conjugation assay to probe the effects of directed mutagenesis on TraT. Our analysis provides no support for the idea that TraT has specific interactions with partner proteins. Instead, we infer that TraT is most likely to function by physical interference with conjugation. This work provides structural insight into a natural inhibitor of microbial gene transfer.
Chen et al. determined the cryo-EM structure of the TraT exclusion protein from the F plasmid of
E. coli
, revealing a unique hollow homodecameric architecture that includes α-helices traversing the outer membrane. Their work indicates that TraT might limit plasmid transfer via physical interference, offering insights into controlling antimicrobial resistance.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/35
/ Bacterial Outer Membrane Proteins - chemistry
/ Bacterial Outer Membrane Proteins - genetics
/ Bacterial Outer Membrane Proteins - metabolism
/ Biomedical and Life Sciences
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Escherichia coli Proteins - ultrastructure
/ Ligands
/ Lipids
/ Plasmids
/ Proteins
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