8ZWS
Mtb. MazF-mt3 toxin in compleex with its antitoxin fragmant
Summary for 8ZWS
| Entry DOI | 10.2210/pdb8zws/pdb |
| Descriptor | Endoribonuclease MazF6, Antitoxin MazE6 (2 entities in total) |
| Functional Keywords | ta system, mazf, mycobacterium tubercolysis, rnase, toxin |
| Biological source | Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) More |
| Total number of polymer chains | 5 |
| Total formula weight | 46229.63 |
| Authors | |
| Primary citation | Tang, Z.,Jiang, P.,Xie, W. Long Dynamic beta 1-beta 2 Loops in M. tb MazF Toxins Affect the Interaction Modes and Strengths of the Toxin-Antitoxin Pairs. Int J Mol Sci, 25:-, 2024 Cited by PubMed Abstract: Tuberculosis is a worldwide plague caused by the pathogen (). Toxin-antitoxin (TA) systems are genetic elements abundantly present in prokaryotic organisms and regulate important cellular processes. MazEF is a TA system implicated in the formation of "persisters cells" of , which contain more than 10 such members. However, the exact function and inhibition mode of each MazF are not fully understood. Here we report crystal structures of MazF-mt3 in its apo form and in complex with the C-terminal half of MazE-mt3. Structural analysis suggested that two long but disordered β1-β2 loops would interfere with the binding of the cognate MazE-mt3 antitoxin. Similar loops are also present in the MazF-mt1 and -mt9 but are sustainably shortened in other MazF members, and these TA pairs behave distinctly in terms of their binding modes and their RNase activities. Systematic crystallographic and biochemical studies further revealed that the biochemical activities of toxins were combined results between the interferences from the characteristic loops and the electrostatic interactions between the cognate TA pairs. This study provides structural insight into the binding mode and the inhibition mechanism of the MazE/F TA pairs, which facilitate the structure-based peptide designs. PubMed: 39273577DOI: 10.3390/ijms25179630 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.27 Å) |
Structure validation
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