Publication Abstract from PubMed
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.
The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface.,Chak KF, Safo MK, Ku WY, Hsieh SY, Yuan HS Proc Natl Acad Sci U S A. 1996 Jun 25;93(13):6437-42. PMID:8692833[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
