4b09 | pdb_00004b09

Structure of unphosphorylated BaeR dimer

spinqualitylabelsall models 4b09, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b09 is a 12 chain structure with sequence from Escherichia coli mg1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TBR NonStd Res: CAS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BAER_ECOL6] Member of the two-component regulatory system BaeS/BaeR. Activates the mdtABCD operon (By similarity). Publication Abstract from PubMed Bacterial 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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