2J48
NMR structure of the pseudo-receiver domain of the CikA protein.
Summary for 2J48
| Entry DOI | 10.2210/pdb2j48/pdb |
| NMR Information | BMRB: 6438 |
| Descriptor | TWO-COMPONENT SENSOR KINASE (1 entity in total) |
| Functional Keywords | kinase, pseudo-receiver, circadian clock, transferase, response regulator, histidine protein kinase |
| Biological source | SYNECHOCOCCUS ELONGATUS |
| Total number of polymer chains | 1 |
| Total formula weight | 12884.99 |
| Authors | Gao, T.,Zhang, X.,Golden, S.S.,LiWang, A. (deposition date: 2006-08-26, release date: 2007-03-06, Last modification date: 2024-05-15) |
| Primary citation | Gao, T.,Zhang, X.,Ivleva, N.B.,Golden, S.S.,LiWang, A. NMR structure of the pseudo-receiver domain of CikA. Protein Sci., 16:465-475, 2007 Cited by PubMed Abstract: The circadian input kinase (CikA) is a major element of the pathway that provides environmental information to the circadian clock of the cyanobacterium Synechococcus elongatus. CikA is a polypeptide of 754 residues and has three recognizable domains: GAF, histidine protein kinase, and receiver-like. This latter domain of CikA lacks the conserved phospho-accepting aspartyl residue of bona fide receiver domains and is thus a pseudo-receiver (PsR). Recently, it was shown that the PsR domain (1) attenuates the autokinase activity of CikA, (2) is necessary to localize CikA to the cell pole, and (3) is necessary for the destabilization of CikA in the presence of the quinone analog 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB). The solution structure of the PsR domain of CikA, CikAPsR, is presented here. A model of the interaction between the PsR domain and HPK portion of CikA provides a potential explanation for how the PsR domain attenuates the autokinase activity of CikA. Finally, a likely quinone-binding surface on CikAPsR is shown here. PubMed: 17322531DOI: 10.1110/ps.062532007 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
