Summary information and primary citation
- PDB-id
-
2mru;
SNAP-derived features in text and
JSON formats
- Class
- DNA binding protein-DNA
- Method
- NMR
- Summary
- Structure of truncated ecmaze-DNA complex
- Reference
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Zorzini V, Buts L, Schrank E, Sterckx YG, Respondek M,
Engelberg-Kulka H, Loris R, Zangger K, van Nuland NA
(2015): "Escherichia
coli antitoxin MazE as transcription factor: insights
into MazE-DNA binding." Nucleic Acids Res.,
43, 1241-1256. doi: 10.1093/nar/gku1352.
- Abstract
- Toxin-antitoxin (TA) modules are pairs of genes
essential for bacterial regulation upon environmental
stresses. The mazEF module encodes the MazF toxin and its
cognate MazE antitoxin. The highly dynamic MazE possesses
an N-terminal DNA binding domain through which it can
negatively regulate its own promoter. Despite being one of
the first TA systems studied, transcriptional regulation of
Escherichia coli mazEF remains poorly understood. This
paper presents the solution structure of C-terminal
truncated E. coli MazE and a MazE-DNA model with a DNA
palindrome sequence ∼ 10 bp upstream of the mazEF promoter.
The work has led to a transcription regulator-DNA model,
which has remained elusive thus far in the E. coli
toxin-antitoxin family. Multiple complementary techniques
including NMR, SAXS and ITC show that the long
intrinsically disordered C-termini in MazE, required for
MazF neutralization, does not affect the interactions
between the antitoxin and its operator. Rather, the MazE
C-terminus plays an important role in the MazF binding,
which was found to increase the MazE affinity for the
palindromic single site operator.
