4KP4
Deciphering cis-trans directionality and visualizing autophosphorylation in histidine kinases.
Summary for 4KP4
| Entry DOI | 10.2210/pdb4kp4/pdb |
| Descriptor | Osmolarity sensor protein EnvZ, Histidine kinase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | four helix-bundle, bergerat fold, kinase and phosphotransferase, atp binding, transferase-signaling protein complex, transferase/signaling protein |
| Biological source | Escherichia coli More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P0AEJ4 |
| Total number of polymer chains | 2 |
| Total formula weight | 52625.43 |
| Authors | Casino, P.,Miguel-Romero, L.,Marina, A. (deposition date: 2013-05-13, release date: 2014-02-12, Last modification date: 2024-02-28) |
| Primary citation | Casino, P.,Miguel-Romero, L.,Marina, A. Visualizing autophosphorylation in histidine kinases. Nat Commun, 5:3258-3258, 2014 Cited by PubMed Abstract: Reversible protein phosphorylation is the most widespread regulatory mechanism in signal transduction. Autophosphorylation in a dimeric sensor histidine kinase is the first step in two-component signalling, the predominant signal-transduction device in bacteria. Despite being the most abundant sensor kinases in nature, the molecular bases of the histidine kinase autophosphorylation mechanism are still unknown. Furthermore, it has been demonstrated that autophosphorylation can occur in two directions, cis (intrasubunit) or trans (intersubunit) within the dimeric histidine kinase. Here, we present the crystal structure of the complete catalytic machinery of a chimeric histidine kinase. The structure shows an asymmetric histidine kinase dimer where one subunit is caught performing the autophosphorylation reaction. A structure-guided functional analysis on HK853 and EnvZ, two prototypical cis- and trans-phosphorylating histidine kinases, has allowed us to decipher the catalytic mechanism of histidine kinase autophosphorylation, which seems to be common independently of the reaction directionality. PubMed: 24500224DOI: 10.1038/ncomms4258 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
