Summary information and primary citation
- PDB-id
-
7wnr;
DSSR-derived features in text and
JSON formats
- Class
- antitoxin-DNA
- Method
- NMR
- Summary
- Data-driven haddock model of mycobacterial
nmaze6-operator DNA complex
- Reference
-
Kumari K, Sarma SP (2022): "Structural
and mutational analysis of MazE6-operator DNA complex
provide insights into autoregulation of toxin-antitoxin
systems." Commun Biol, 5,
963. doi: 10.1038/s42003-022-03933-5.
- Abstract
- Of the 10 paralogs of MazEF Toxin-Antitoxin system in
Mycobacterium tuberculosis, MazEF6 plays an important role
in multidrug tolerance, virulence, stress adaptation and
Non Replicative Persistant (NRP) state establishment. The
solution structures of the DNA binding domain of MazE6 and
of its complex with the cognate operator DNA show that
transcriptional regulation occurs by binding of MazE6 to an
18 bp operator sequence bearing the TANNNT motif (-10
region). Kinetics and thermodynamics of association, as
determined by NMR and ITC, indicate that the nMazE6-DNA
complex is of high affinity. Residues in N-terminal region
of MazE6 that are key for its homodimerization, DNA binding
specificity, and the base pairs in the operator DNA
essential for the protein-DNA interaction, have been
identified. It provides a basis for design of
chemotherapeutic agents that will act via disruption of TA
autoregulation, leading to cell death.
