2w0n

Plasticity of PAS domain and potential role for signal transduction in the histidine-kinase DcuS

spinqualitylabelsall models 2w0n, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w0n is a 1 chain structure with sequence from Escherichia coli bl21(de3). Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1ojg Activity: Histidine kinase, with EC number 2.7.13.3 Resources: FirstGlance, OCA, RCSB, PDBsum Function [DCUS_ECOLI] Member of the two-component regulatory system DcuR/DcuS. Involved in the C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN; dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic C4-dicarboxylate transporter dctA. Activates DcuR by phosphorylation. 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 The mechanistic understanding of how membrane-embedded sensor kinases recognize signals and regulate kinase activity is currently limited. Here we report structure-function relationships of the multidomain membrane sensor kinase DcuS using solid-state NMR, structural modeling and mutagenesis. Experimental data of an individual cytoplasmic Per-Arnt-Sim (PAS) domain were compared to structural models generated in silico. These studies, together with previous NMR work on the periplasmic PAS domain, enabled structural investigations of a membrane-embedded 40-kDa construct by solid-state NMR, comprising both PAS segments and the membrane domain. Structural alterations are largely limited to protein regions close to the transmembrane segment. Data from isolated and multidomain constructs favor a disordered N-terminal helix in the cytoplasmic domain. Mutations of residues in this region strongly influence function, suggesting that protein flexibility is related to signal transduction toward the kinase domain and regulation of kinase activity. Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS.,Etzkorn M, Kneuper H, Dunnwald P, Vijayan V, Kramer J, Griesinger C, Becker S, Unden G, Baldus M Nat Struct Mol Biol. 2008 Oct;15(10):1031-9. Epub 2008 Sep 28. PMID:18820688 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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