1UB4
crystal structure of MazEF complex
Summary for 1UB4
Entry DOI | 10.2210/pdb1ub4/pdb |
Descriptor | MazF protein, MazE protein (3 entities in total) |
Functional Keywords | toxin, antidote, programmed cell death, post-segregation, addiction module, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, dna binding protein |
Biological source | Escherichia coli More |
Total number of polymer chains | 3 |
Total formula weight | 33620.67 |
Authors | Kamada, K.,Hanaoka, F.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-03-28, release date: 2003-05-20, Last modification date: 2023-12-27) |
Primary citation | Kamada, K.,Hanaoka, F.,Burley, S.K. Crystal Structure of the MazE/MazF Complex. Molecular Bases of Antidote-Toxin Recognition Mol.Cell, 11:875-884, 2003 Cited by PubMed 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. PubMed: 12718874DOI: 10.1016/S1097-2765(03)00097-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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