4CB0
Crystal structure of CpxAHDC in complex with ATP (hexagonal form)
Summary for 4CB0
| Entry DOI | 10.2210/pdb4cb0/pdb |
| Related | 4BIU 4BIV 4BIW 4BIX 4BIY 4BIZ |
| Descriptor | SENSOR PROTEIN CPXA, ADENOSINE-5'-TRIPHOSPHATE, SULFATE ION (3 entities in total) |
| Functional Keywords | transferase, signal transduction, two-components systems, histidine kinases |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cell inner membrane ; Multi-pass membrane protein : P0AE82 |
| Total number of polymer chains | 2 |
| Total formula weight | 68937.97 |
| Authors | Mechaly, A.E.,Sassoon, N.,Betton, J.M.,Alzari, P.M. (deposition date: 2013-10-09, release date: 2014-02-12, Last modification date: 2017-07-12) |
| Primary citation | Mechaly, A.E.,Sassoon, N.,Betton, J.M.,Alzari, P.M. Segmental Helical Motions and Dynamical Asymmetry Modulate Histidine Kinase Autophosphorylation. Plos Biol., 12:1776-, 2014 Cited by PubMed Abstract: Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP domain to control the transient interaction between the histidine-containing and ATP-binding domains during the catalytic reaction. Here we report crystal structures of the full cytoplasmic region of CpxA, a prototypical HK involved in Escherichia coli response to envelope stress. The structural ensemble, which includes the Michaelis complex, unveils HK activation as a highly dynamic process, in which HAMP modulates the segmental mobility of the central HK α-helices to promote a strong conformational and dynamical asymmetry that characterizes the kinase-active state. A mechanical model based on our structural and biochemical data provides insights into HAMP-mediated signal transduction, the autophosphorylation reaction mechanism, and the symmetry-dependent control of HK kinase/phosphatase functional states. PubMed: 24492262DOI: 10.1371/JOURNAL.PBIO.1001776 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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