1cei: Difference between revisions

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[[Image:1cei.gif|left|200px]]
{{Seed}}
[[Image:1cei.png|left|200px]]


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{{STRUCTURE_1cei|  PDB=1cei  |  SCENE=  }}  
{{STRUCTURE_1cei|  PDB=1cei  |  SCENE=  }}  


'''STRUCTURE DETERMINATION OF THE COLICIN E7 IMMUNITY PROTEIN (IMME7) THAT BINDS SPECIFICALLY TO THE DNASE-TYPE COLICIN E7 AND INHIBITS ITS BACTERIOCIDAL ACTIVITY'''
===STRUCTURE DETERMINATION OF THE COLICIN E7 IMMUNITY PROTEIN (IMME7) THAT BINDS SPECIFICALLY TO THE DNASE-TYPE COLICIN E7 AND INHIBITS ITS BACTERIOCIDAL ACTIVITY===




==Overview==
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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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{{ABSTRACT_PUBMED_8692833}}


==About this Structure==
==About this Structure==
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[[Category: Yuan, H S.]]
[[Category: Yuan, H S.]]
[[Category: Immunity protein]]
[[Category: Immunity protein]]
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