Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA
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Title
Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA
Authors
Keywords
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Journal
MICROBIOLOGY-SGM
Volume 161, Issue 3, Pages 503-515
Publisher
Microbiology Society
Online
2014-12-24
DOI
10.1099/mic.0.000024
References
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Note: Only part of the references are listed.- Colicin import into E. coli cells: A model system for insights into the import mechanisms of bacteriocins
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- The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein
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- Proline Substitution of Dimer Interface β-strand Residues as a Strategy for the Design of Functional Monomeric Proteins
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- Crystal Structures of a CTXφ pIII Domain Unbound and in Complex with aVibrio choleraeTolA Domain Reveal Novel Interaction Interfaces
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- Low Resolution Structure and Dynamics of a Colicin-Receptor Complex Determined by Neutron Scattering
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- The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins
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- Genome-wide screens: novel mechanisms in colicin import and cytotoxicity
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- (2008) Yang Zhang BMC BIOINFORMATICS
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- Differential complementation of ÎtolA Escherichia coliby aYersinia enterocoliticaTolA homologue
- (2008) Alicia C. Weitzel et al. FEMS MICROBIOLOGY LETTERS
- The Jpred 3 secondary structure prediction server
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