2W0N
Plasticity of PAS domain and potential role for signal transduction in the histidine-kinase DcuS
Summary for 2W0N
| Entry DOI | 10.2210/pdb2w0n/pdb |
| Related | 1OJG |
| Descriptor | SENSOR PROTEIN DCUS (1 entity in total) |
| Functional Keywords | signal transduction, two-component regulatory system, pas, dcus, kinase, membrane, transferase, solid state nmr, cell inner membrane, cell membrane, transmembrane, phosphoprotein |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P0AEC8 |
| Total number of polymer chains | 1 |
| Total formula weight | 13283.90 |
| Authors | Etzkorn, M.,Kneuper, H.,Duennwald, P.,Vijayan, V.,Kraemer, J.,Griesinger, C.,Becker, S.,Unden, G.,Baldus, M. (deposition date: 2008-08-19, release date: 2008-09-30, Last modification date: 2024-05-15) |
| Primary citation | Etzkorn, M.,Kneuper, H.,Duennwald, P.,Vijayan, V.,Kraemer, J.,Griesinger, C.,Becker, S.,Unden, G.,Baldus, M. Plasticity of the Pas Domain and a Potential Role for Signal Transduction in the Histidine Kinase Dcus. Nat.Struct.Mol.Biol., 15:1031-, 2008 Cited by PubMed Abstract: 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. PubMed: 18820688DOI: 10.1038/NSMB.1493 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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