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. 1996 Jun 25;93(13):6437–6442. doi: 10.1073/pnas.93.13.6437

The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface.

K F Chak 1, M K Safo 1, W Y Ku 1, S Y Hsieh 1, H S Yuan 1
PMCID: PMC39041  PMID: 8692833

Abstract

The immunity protein of colicin E7 (ImmE7) can bind specifically to the DNase-type colicin E7 and inhibit its bactericidal activity. Here we report the 1.8-angstrom crystal structure of the ImmE7 protein. This is the first x-ray structure determined in the superfamily of colicin immunity proteins. The ImmE7 protein consists of four antiparallel alpha-helices, folded in a topology similar to the architecture of a four-helix bundle structure. A region rich in acidic residues is identified. This negatively charged area has the greatest variability within the family of DNase-type immunity proteins; thus, it seems likely that this area is involved in specific binding to colicin. Based on structural, genetic, and kinetic data, we suggest that all the DNase-type immunity proteins, as well as colicins, share a "homologous-structural framework" and that specific interaction between a colicin and its cognate immunity protein relies upon how well these two proteins' charged residues match on the interaction surface, thus leading to specific immunity of the colicin.

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Selected References

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