4MDX
Crystal structure of Bacillus subtilis MazF in complex with RNA
Summary for 4MDX
| Entry DOI | 10.2210/pdb4mdx/pdb |
| Descriptor | mRNA interferase EndoA, RNA, mRNA, IODIDE ION, ... (5 entities in total) |
| Functional Keywords | toxin-antitoxin complex, toxin-mrna complex, mazf, mrna interferase, endoa, ydce, toxin, antitoxin, maze, hydrolase-rna complex, hydrolase/rna |
| Biological source | Bacillus subtilis subsp. subtilis More |
| Total number of polymer chains | 3 |
| Total formula weight | 29732.17 |
| Authors | Simanshu, D.K.,Patel, D.J. (deposition date: 2013-08-23, release date: 2013-10-23, Last modification date: 2024-02-28) |
| Primary citation | Simanshu, D.K.,Yamaguchi, Y.,Park, J.H.,Inouye, M.,Patel, D.J. Structural Basis of mRNA Recognition and Cleavage by Toxin MazF and Its Regulation by Antitoxin MazE in Bacillus subtilis. Mol.Cell, 52:447-458, 2013 Cited by PubMed Abstract: MazF is an mRNA interferase, which, upon activation during stress conditions, cleaves mRNAs in a sequence-specific manner, resulting in cellular growth arrest. During normal growth conditions, the MazF toxin is inactivated through binding to its cognate antitoxin, MazE. How MazF specifically recognizes its mRNA target and carries out cleavage and how the formation of the MazE-MazF complex inactivates MazF remain unclear. We present crystal structures of MazF in complex with mRNA substrate and antitoxin MazE in Bacillus subtilis. The structure of MazF in complex with uncleavable UUdUACAUAA RNA substrate defines the molecular basis underlying the sequence-specific recognition of UACAU and the role of residues involved in the cleavage through site-specific mutational studies. The structure of the heterohexameric (MazF)2-(MazE)2-(MazF)2 complex in Bacillus subtilis, supplemented by mutational data, demonstrates that the positioning of the C-terminal helical segment of MazE within the RNA-binding channel of the MazF dimer prevents mRNA binding and cleavage by MazF. PubMed: 24120662DOI: 10.1016/j.molcel.2013.09.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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