Structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus.
Acta Crystallogr D Biol Crystallogr
; 71(Pt 8): 1768-76, 2015 Aug.
Article
in En
| MEDLINE
| ID: mdl-26249357
ABSTRACT
The SaeR/S two-component regulatory system is essential for controlling the expression of many virulence factors in Staphylococcus aureus. SaeR, a member of the OmpR/PhoB family, is a response regulator with an N-terminal regulatory domain and a C-terminal DNA-binding domain. In order to elucidate how SaeR binds to the promoter regions of target genes, the crystal structure of the DNA-binding domain of SaeR (SaeR(DBD)) was solved at 2.5 Å resolution. The structure reveals that SaeR(DBD) exists as a monomer and has the canonical winged helix-turn-helix module. EMSA experiments suggested that full-length SaeR can bind to the P1 promoter and that the binding affinity is higher than that of its C-terminal DNA-binding domain. Five key residues on the winged helix-turn-helix module were verified to be important for binding to the P1 promoter in vitro and for the physiological function of SaeR in vivo.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Staphylococcal Infections
/
Staphylococcus aureus
/
Bacterial Proteins
/
DNA-Binding Proteins
Limits:
Humans
Language:
En
Journal:
Acta Crystallogr D Biol Crystallogr
Year:
2015
Type:
Article