Title: Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition. | Journal: Molecular cell. 2003 Apr;11(4):875-84 | Authors: Kamada K, Hanaoka F, Burley SK. | Abstract: A structure of the Escherichia coli chromosomal MazE/MazF addiction module has been determined at 1.7 A resolution. Addiction modules consist of stable toxin and unstable antidote proteins that govern bacterial cell death. MazE (antidote) and MazF (toxin) form a linear heterohexamer composed of alternating toxin and antidote homodimers (MazF(2)-MazE(2)-MazF(2)). The MazE homodimer contains a beta barrel from which two extended C termini project, making interactions with flanking MazF homodimers that resemble the plasmid-encoded toxins CcdB and Kid. The MazE/MazF heterohexamer structure documents that the mechanism of antidote-toxin recognition is common to both chromosomal and plasmid-borne addiction modules, and provides general molecular insights into toxin function, antidote degradation in the absence of toxin, and promoter DNA binding by antidote/toxin complexes. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/12718874 |
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