4B09

Structure of unphosphorylated BaeR dimer

Summary for 4B09

• Entry DOI: 10.2210/pdb4b09/pdb
• Descriptor: TRANSCRIPTIONAL REGULATORY PROTEIN BAER, HEXATANTALUM DODECABROMIDE (2 entities in total)
• Functional Keywords: transcription, response regulator, dna binding
• Biological source: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655
• Cellular location: Cytoplasm (Potential): P69229
• Total number of polymer chains: 12
• Total formula weight: 353572.89

Authors

Choudhury, H.,Beis, K. (deposition date: 2012-06-29, release date: 2013-07-10, Last modification date: 2024-11-13)

Primary citation

Choudhury, H.G.,Beis, K.
The Dimeric Form of the Unphosphorylated Response Regulator Baer.
Protein Sci., 22:1287-, 2013

PubMed Abstract: Bacterial response regulators (RRs) can regulate the expression of genes that confer antibiotic resistance; they contain a receiver and an effector domain and their ability to bind DNA is based on the dimerization state. This is triggered by phosphorylation of the receiver domain by a kinase. However, even in the absence of phosphorylation RRs can exist in equilibrium between monomers and dimers with phosphorylation shifting the equilibrium toward the dimer form. We have determined the crystal structure of the unphosphorylated dimeric BaeR from Escherichia coli. The dimer interface is formed by a domain swap at the receiver domain. In comparison with the unphosphorylated dimeric PhoP from Mycobacterium tuberculosis, BaeR displays an asymmetry of the effector domains.

PubMed: 23868292
DOI: 10.1002/PRO.2311

Experimental method

X-RAY DIFFRACTION (3.3 Å)