6A6X

The crystal structure of the Mtb MazE-MazF-mt9 complex

Summary for 6A6X

• Entry DOI: 10.2210/pdb6a6x/pdb
• Descriptor: Probable endoribonuclease MazF7, Antitoxin MazE7, SULFATE ION, ... (4 entities in total)
• Functional Keywords: mycobacterium tuberculosis, toxin-antitoxin system, toxin
• Biological source: Mycobacterium tuberculosis; More
• Total number of polymer chains: 4
• Total formula weight: 47581.46

Authors

Xie, W.,Chen, R.,Tu, J. (deposition date: 2018-06-29, release date: 2019-07-03, Last modification date: 2023-11-22)

Primary citation

Chen, R.,Tu, J.,Tan, Y.,Cai, X.,Yang, C.,Deng, X.,Su, B.,Ma, S.,Liu, X.,Ma, P.,Du, C.,Xie, W.
Structural and Biochemical Characterization of the Cognate and Heterologous Interactions of the MazEF-mt9 TA System.
Acs Infect Dis., 5:1306-1316, 2019

PubMed Abstract: Toxin-antitoxin (TA) modules widely exist in bacteria, and their activities are associated with the persister phenotype of the pathogen (). causes tuberculosis, a contagious and severe airborne disease. There are 10 MazEF TA systems in that play important roles in stress adaptation. How the antitoxins antagonize toxins in or how the 10 TA systems crosstalk to each other are of interest, but the detailed molecular mechanisms are largely unclear. MazEF-mt9 is a unique member among the MazEF family due to its tRNase activity, which is usually carried out by the VapC toxins. Here, we present the cocrystal structure of the MazEF-mt9 complex at 2.7 Å. By characterizing the association mode between the TA pairs through various techniques, we found that MazF-mt9 bound not only its cognate antitoxin but also the noncognate antitoxin MazE-mt1, a phenomenon that could be also observed in vivo. Based on our structural and biochemical work, we propose that the cognate and heterologous interactions among different TA systems work together in vivo to relieve the toxicity of MazF-mt9 toward cells.

PubMed: 31267737
DOI: 10.1021/acsinfecdis.9b00001

Experimental method

X-RAY DIFFRACTION (2.7 Å)