Structural basis of toxicity and immunity in contact-dependent growth inhibition (CDI) systems
作者： R. P. Morse , K. C. Nikolakakis , J. L. E. Willett , E. Gerrick , D. A. Low
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摘要: Contact-dependent growth inhibition (CDI) systems encode polymorphic toxin/immunity proteins that mediate competition between neighboring bacterial cells. We present crystal structures of CDI complexes from Escherichia coli EC869 and Burkholderia pseudomallei 1026b. Despite sharing little sequence identity, the toxin domains are structurally similar have homology to endonucleases. The is a Zn2+-dependent DNase capable completely degrading genomes target cells, whereas Bp1026b cleaves aminoacyl acceptor stems tRNA molecules. Each immunity protein binds inactivates its cognate in unique manner. complex stabilized through an unusual β-augmentation interaction. In contrast, exploits shape charge complementarity occlude active site. These represent initial glimpse into network, illustrating how sequence-diverse toxins adopt convergent folds yet retain distinct binding interactions with proteins. Moreover, we visual demonstration delivery cell.
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