PMID:12718874
| Citation |
Kamada, K, Hanaoka, F and Burley, SK (2003) Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition. Mol. Cell 11:875-84 |
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| 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. |
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| Keywords |
Antidotes/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacterial Toxins/chemistry; Bacterial Toxins/genetics; Bacterial Toxins/metabolism; Cell Death/genetics; Chromosomes, Bacterial/genetics; Chromosomes, Bacterial/metabolism; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Endoribonucleases; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial/genetics; Macromolecular Substances; Molecular Conformation; Molecular Sequence Data; Molecular Structure; Plasmids/genetics; Plasmids/metabolism; Prokaryotic Cells/metabolism; Protein Structure, Tertiary/physiology; Sequence Homology, Amino Acid |
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