5IUL
Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3
Summary for 5IUL
| Entry DOI | 10.2210/pdb5iul/pdb |
| Related | 5IUJ 5IUK 5IUM 5IUN |
| Descriptor | Sensor histidine kinase DesK, Transcriptional regulatory protein DesR, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (6 entities in total) |
| Functional Keywords | two-component regulatory system, kinase, response regulator, phosphotransfer complex, phosphotransfer, transferase |
| Biological source | Bacillus subtilis More |
| Cellular location | Cell membrane ; Multi-pass membrane protein : O34757 Cytoplasm : O34723 |
| Total number of polymer chains | 6 |
| Total formula weight | 132287.95 |
| Authors | Trajtenberg, F.,Imelio, J.A.,Larrieux, N.,Buschiazzo, A. (deposition date: 2016-03-18, release date: 2016-12-21, Last modification date: 2024-03-06) |
| 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 (3.153 Å) |
Structure validation
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