Concerted Folding and Binding of a Flexible Colicin Domain to Its Periplasmic Receptor TolA
Open Access
- 1 June 2003
- journal article
- Published by Elsevier
- Vol. 278 (24) , 21860-21868
- https://doi.org/10.1074/jbc.m300411200
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Local dispersal promotes biodiversity in a real-life game of rock–paper–scissorsNature, 2002
- Macromolecular Import into Escherichia coli: The TolA C-Terminal Domain Changes Conformation When Interacting with the Colicin A ToxinBiochemistry, 2002
- The TolA-recognition Site of Colicin N. ITC, SPR and Stopped-flow Fluorescence Define a Crucial 27-residue SegmentJournal of Molecular Biology, 2000
- Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolAStructure, 1999
- Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 Å: evidence for conformational lability 1 1Edited by J. M. ThorntonJournal of Molecular Biology, 1999
- Crystal structure of a colicin N fragment suggests a model for toxicityStructure, 1998
- Discovery of critical Tol A‐binding residues in the bactericidal toxin colicin N: a biophysical approachMolecular Microbiology, 1998
- The TolA protein interacts with colicin E1 differently than with other group A colicinsJournal of Bacteriology, 1997
- The biology of E colicins: paradigms and paradoxesMicrobiology, 1996
- Nucleotide sequencing of the structural gene for colicin N reveals homology between the catalytic, C‐terminal domains of colicins A and NMolecular Microbiology, 1987