The long and short of colicin action: the molecular basis for the biological activity of channel-forming colicins.
Channel-forming colicins undergo a remarkable series of conformational gyrations during their voyage from the extracellular milieu to the periplasmic membrane. Crystal structures of the intact colicin la molecule and a channel-forming domain of colicin E1 illuminate relationships between the molecular structure and biological function of these voltage-dependent channel-forming toxins.
Gouaux
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Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. jeg52@columbia.edu
D001426:Bacterial Proteins / Q000378:metabolism; D001692:Biological Transport; D003087:Colicins / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins; D015640:Ion Channel Gating; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000378:metabolism; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D003087:Colicins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; C028593:colicin receptor, E coli; C062093:tolA protein, E coli; C057616:tonB protein, Bacteria; C489181:tonB protein, E coli