4QWQ

Crystal structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus

Summary for 4QWQ

• Entry DOI: 10.2210/pdb4qwq/pdb
• Descriptor: Response regulator SaeR (2 entities in total)
• Functional Keywords: winged helix-turn-helix, gene expression regulation, dna, transcription regulator
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 26487.82

Authors

Fan, X.,Zhu, Y.,Zhang, X.,Teng, M.,Li, X. (deposition date: 2014-07-17, release date: 2015-08-19, Last modification date: 2024-03-20)

Primary citation

Fan, X.,Zhang, X.,Zhu, Y.,Niu, L.,Teng, M.,Sun, B.,Li, X.
Structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus.
Acta Crystallogr.,Sect.D, 71:1768-1776, 2015

PubMed 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.

PubMed: 26249357
DOI: 10.1107/S1399004715010287

Experimental method

X-RAY DIFFRACTION (2.501 Å)