Summary information and primary citation
- PDB-id
-
9ill;
DSSR-derived features in text and
JSON formats
- Class
- DNA binding protein
- Method
- NMR
- Summary
- Monomeric sara-e89q in complex with DNA
- Reference
-
Xia B, Fu DH (2023): "solution
Structure of the monomeric SarA in complex with DNA."
Biomol.NMR Assign, 17, 193-197.
doi: 10.1007/s12104-023-10140-8.
- Abstract
- SarA is a global transcription regulator in S. aureus
which regulates the expression of over 120 genes related to
quorum sensing, biofilm synthesis, drug resistance and many
other important physiological processes during host
infection. SarA can bind to the promoter region of agr and
other target genes to activate or repress the
transcription. The crystal structure of SarA uncovered a
MarR protein-like conformation with two symmetrical winged
helix domains, while its DNA binding mechanism is still
unknown. We have constructed a monomeric DNA binding domain
of SarA (SarA<sub>ΔN19</sub>) for the study of
the interaction between SarA and DNA with NMR spectroscopy.
Here, we report the <sub>1</sub>H,
<sub>13</sub>C and <sub>15</sub>N
NMR assignment of SarA<sub>ΔN19</sub>/DNA
complex which is the first step towards further structure
and function analysis.
