5IUM
Crystal structure of phosphorylated DesKC
Summary for 5IUM
| Entry DOI | 10.2210/pdb5ium/pdb |
| Related | 3GIG 5IUJ 5IUK 5IUL 5IUM |
| Descriptor | Sensor histidine kinase DesK, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | four-helix bundle, ghl atpase domain, cell membrane, kinase, membrane, phosphoprotein, transferase, transmembrane, two-component regulatory system |
| Biological source | Bacillus subtilis |
| Cellular location | Cell membrane ; Multi-pass membrane protein : O34757 |
| Total number of polymer chains | 2 |
| Total formula weight | 51240.31 |
| Authors | Trajtenberg, F.,Buschiazzo, A. (deposition date: 2016-03-18, release date: 2016-12-21, Last modification date: 2023-09-27) |
| Primary citation | Trajtenberg, F.,Imelio, J.A.,Machado, M.R.,Larrieux, N.,Marti, M.A.,Obal, G.,Mechaly, A.E.,Buschiazzo, A. Regulation of signaling directionality revealed by 3D snapshots of a kinase:regulator complex in action. Elife, 5:-, 2016 Cited by PubMed Abstract: Two-component systems (TCS) are protein machineries that enable cells to respond to input signals. Histidine kinases (HK) are the sensory component, transferring information toward downstream response regulators (RR). HKs transfer phosphoryl groups to their specific RRs, but also dephosphorylate them, overall ensuring proper signaling. The mechanisms by which HKs discriminate between such disparate directions, are yet unknown. We now disclose crystal structures of the HK:RR complex DesK:DesR from , comprising snapshots of the phosphotransfer and the dephosphorylation reactions. The HK dictates the reactional outcome through conformational rearrangements that include the reactive histidine. The phosphotransfer center is asymmetric, poised for dissociative nucleophilic substitution. The structural bases of HK phosphatase/phosphotransferase control are uncovered, and the unexpected discovery of a dissociative reactional center, sheds light on the evolution of TCS phosphotransfer reversibility. Our findings should be applicable to a broad range of signaling systems and instrumental in synthetic TCS rewiring. PubMed: 27938660DOI: 10.7554/eLife.21422 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.162 Å) |
Structure validation
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