A 136-amino-acid-residue COOH-terminal fragment of colicin A is endowed with ionophoric activity
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1990.tb15503.x/fullpdf
Reference22 articles.
1. The membrane channel-forming colicin A: synthesis, secretion, structure, action and immunity
2. Isolation, molecular and functional properties of the C-terminal domain of colicin A.
3. Crystallization of the C-terminal domain of colicin A carrying the voltage-dependent pore activity of the protein
4. Structure of the membrane-pore-forming fragment of colicin A
5. Secondary structure of the pore-forming colicin A and its C-terminal fragment. Experimental fact and structure prediction
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1. H1 helix of colicin U causes phospholipid membrane permeation;Biochimica et Biophysica Acta (BBA) - Biomembranes;2022-04
2. Pore-Forming Colicins: Unusual Ion Channels – Unusually Regulated;Springer Series in Biophysics;2015
3. Structural Evidence That Colicin A Protein Binds to a Novel Binding Site of TolA Protein in Escherichia coli Periplasm;Journal of Biological Chemistry;2012-06
4. Interfacial Interactions of Pore-Forming Colicins;Advances in Experimental Medicine and Biology;2010
5. Colicin N Binds to the Periphery of Its Receptor and Translocator, Outer Membrane Protein F;Structure;2008-03
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