4b09
Structure of unphosphorylated BaeR dimer
Structural highlights
FunctionBAER_ECOLI Member of the two-component regulatory system BaeS/BaeR which responds to envelope stress (PubMed:12354228). Activates expression of periplasmic chaperone spy in response to spheroplast formation, indole and P pili protein PapG overexpression (PubMed:12354228). Activates the mdtABCD (PubMed:12107133, PubMed:12107134) and probably the CRISPR-Cas casABCDE-ygbT-ygbF operon (PubMed:21255106).[1] [2] [3] [4] Publication Abstract from PubMedBacterial response regulators 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 response regulators can exist in equilibrium between monomers and dimers with phosphorylation shifting the equilibrium towards 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. The dimeric form of the unphosphorylated response regulator BaeR.,Choudhury HG, Beis K Protein Sci. 2013 Jul 19. doi: 10.1002/pro.2311. PMID:23868292[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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