This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. All colicins can be arranged into three functional domains. The amino terminal region is required for translocation across the outer membrane. The central domain is required for recognition of the outer membrane receptors and the carboxy terminal domain contains the killing activity of the colicin. These killing functions range from endonucleases to inhibition of peptidoglycan synthesis, to deenergizing cytoplasmic membranes by channel formation. Colicin B enters the cell through FepA, kills cells by forming channels in the cytoplasmic membrane. My lab is interested in the killing action of the channel-forming colicins. Much has been determined about the means by which the channel-forming domains of various colicins behave in vitro in lipid bilayers. With B-group colicins, very little work has been done in vivo, and that without benefit of any crystal structures to guide understanding and mutagenesis. Colicin B is thus an excellent candidate for crystallization and our further studies.
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