Journal
STRUCTURE
Volume 10, Issue 10, Pages 1425-1433Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(02)00856-0
Keywords
toxin-antitoxin; plasmid maintenance; postsegregational killing; DNA replication; mutational analysis; CcdB
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We have determined the structure of Kid toxin protein from E. coli plasmid R1 involved in stable plasmid inheritance by postsegregational killing of plasmid-less daughter cells. Kid forms a two-component system with its antagonist, Kis antitoxin. Our 1.4 Angstrom crystal structure of Kid reveals a 2-fold symmetric dimer that closely resembles the DNA gyrase-inhibitory toxin protein CcdB from E. coli F plasmid despite the lack of any notable sequence similarity. Analysis of nontoxic mutants of Kid suggests a target interaction interface associated with toxicity that is in marked contrast to that proposed for CcdB. A possible region for interaction of Kid with the antitoxin is proposed that overlaps with the target binding site and may explain the mode of antitoxin action.
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