5LFK
Crystal structure of CpxAHDC (hemiphosphorylated form)
Summary for 5LFK
| Entry DOI | 10.2210/pdb5lfk/pdb |
| Descriptor | Sensor histidine kinase CpxA, SULFATE ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | two-componet systems, histidine kinase, transferase |
| Biological source | Escherichia coli More |
| Cellular location | Cell inner membrane ; Multi-pass membrane protein : P0AE82 P0AE82 |
| Total number of polymer chains | 2 |
| Total formula weight | 68347.17 |
| Authors | Mechaly, A.E.,Alzari, P.M. (deposition date: 2016-07-01, release date: 2017-06-07, Last modification date: 2024-01-10) |
| Primary citation | Mechaly, A.E.,Soto Diaz, S.,Sassoon, N.,Buschiazzo, A.,Betton, J.M.,Alzari, P.M. Structural Coupling between Autokinase and Phosphotransferase Reactions in a Bacterial Histidine Kinase. Structure, 25:939-944.e3, 2017 Cited by PubMed Abstract: Bacterial two-component systems consist of a sensor histidine kinase (HK) and a response regulator (RR). HKs are homodimers that catalyze the autophosphorylation of a histidine residue and the subsequent phosphoryl transfer to its RR partner, triggering an adaptive response. How the HK autokinase and phosphotransferase activities are coordinated remains unclear. Here, we report X-ray structures of the prototypical HK CpxA trapped as a hemi-phosphorylated dimer, and of the receiver domain from the RR partner, CpxR. Our results reveal that the two catalytic reactions can occur simultaneously, one in each protomer of the asymmetric CpxA dimer. Furthermore, the increase of autokinase activity in the presence of phosphotransfer-impaired CpxR put forward the idea of an allosteric switching mechanism, according to which CpxR binding to one CpxA protomer triggers autophosphorylation in the second protomer. The ensuing dynamical model provides a mechanistic explanation of how HKs can efficiently orchestrate two catalytic reactions involving large-scale protein motions. PubMed: 28552574DOI: 10.1016/j.str.2017.04.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.094 Å) |
Structure validation
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