1zh4

Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE

spinqualitylabelsall models 1zh4, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zh4 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BEF, MG Related: 1zh2, 1zh3 Gene: kdpE ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [KDPE_ECOLI] Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacterial response regulators are key regulatory proteins that function as the final elements of so-called two-component signaling systems. The activities of response regulators in vivo are modulated by phosphorylation that results from interactions between the response regulator and its cognate histidine protein kinase. The level of response regulator phosphorylation, which is regulated by intra-or extracellular signals sensed by the histidine protein kinase, ultimately determines the output response that is initiated or carried out by the response regulator. We have recently hypothesized that in the OmpR/PhoB subfamily of response regulator transcription factors, this activation involves a common mechanism of dimerization using a set of highly conserved residues in the alpha4-beta5-alpha5 face. Here we report the X-ray crystal structures of the regulatory domains of response regulators TorR (1.8 A), Ca(2+)-bound KdpE (2.0 A), and Mg(2+)/BeF(3)(-)-bound KdpE (2.2 A), both members of the OmpR/ PhoB subfamily from Escherichia coli. Both regulatory domains form symmetric dimers in the asymmetric unit that involve the alpha4-beta5-alpha5 face. As observed previously in other OmpR/PhoB response regulators, the dimer interfaces are mediated by highly conserved residues within this subfamily. These results provide further evidence that most all response regulators of the OmpR/ PhoB subfamily share a common mechanism of activation by dimerization. A common dimerization interface in bacterial response regulators KdpE and TorR.,Toro-Roman A, Wu T, Stock AM Protein Sci. 2005 Dec;14(12):3077-88. PMID:16322582 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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