Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA
Author:
Publisher
Microbiology Society
Subject
Microbiology
Reference62 articles.
1. Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 Å resolution
2. Concerted Folding and Binding of a Flexible Colicin Domain to Its Periplasmic Receptor TolA
3. A Natively Unfolded Toxin Domain Uses Its Receptor as a Folding Template
4. Uptake across the cell envelope and insertion into the inner membrane of ion channel-forming colicins in E coli
5. Allosteric β-propeller signalling in TolB and its manipulation by translocating colicins
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1. Recruitment of the TolA Protein to Cell Constriction Sites in Escherichia coli via Three Separate Mechanisms, and a Critical Role for FtsWI Activity in Recruitment of both TolA and TolQ;Journal of Bacteriology;2022-01-18
2. Bifurcated binding of the OmpF receptor underpins import of the bacteriocin colicin N into Escherichia coli;Journal of Biological Chemistry;2020-07
3. Cyclic AMP-CRP Modulates the Cell Morphology of Klebsiella pneumoniae in High-Glucose Environment;Frontiers in Microbiology;2020-01-21
4. Template‐based modeling of diverse protein interactions in CAPRI rounds 38‐45;Proteins: Structure, Function, and Bioinformatics;2019-11-21
5. Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells;Protein Secretion in Bacteria;2019-09-12
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