PDBsum entry 2j48

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protein links
Transferase PDB id
Protein chain
119 a.a. *
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Nmr structure of the pseudo-receiver domain of the cika protein.
Structure: Two-component sensor kinase. Chain: a. Fragment: pseudo-receiver domain, residues 627-745. Engineered: yes
Source: Synechococcus elongatus. Organism_taxid: 1140. Strain: pcc 7942. Atcc: 33912. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: de3.
NMR struc: 20 models
Authors: T.Gao,X.Zhang,S.S.Golden,A.Liwang
Key ref:
T.Gao et al. (2007). NMR structure of the pseudo-receiver domain of CikA. Protein Sci, 16, 465-475. PubMed id: 17322531 DOI: 10.1110/ps.062532007
26-Aug-06     Release date:   06-Mar-07    
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Protein chain
Pfam   ArchSchema ?
Q9KHI5  (Q9KHI5_SYNE7) -  Circadian input kinase
754 a.a.
119 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     two-component signal transduction system (phosphorelay)   1 term 


DOI no: 10.1110/ps.062532007 Protein Sci 16:465-475 (2007)
PubMed id: 17322531  
NMR structure of the pseudo-receiver domain of CikA.
T.Gao, X.Zhang, N.B.Ivleva, S.S.Golden, A.LiWang.
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.
  Selected figure(s)  
Figure 7.
Figure 7. A model of the interaction between the PsR domain and HPK portion of CikA. (A) The X-ray crystal structure of the Spo0F--
Figure 8.
Figure 8. Mapping of DBMIB-induced spectral perturbations onto the structure of CikAPsR. The surface of CikAPsR is shown in
  The above figures are reprinted by permission from the Protein Society: Protein Sci (2007, 16, 465-475) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20211578 R.B.Bourret (2010).
Receiver domain structure and function in response regulator proteins.
  Curr Opin Microbiol, 13, 142-149.  
20231482 T.L.Wood, J.Bridwell-Rabb, Y.I.Kim, T.Gao, Y.G.Chang, A.LiWang, D.P.Barondeau, and S.S.Golden (2010).
The KaiA protein of the cyanobacterial circadian oscillator is modulated by a redox-active cofactor.
  Proc Natl Acad Sci U S A, 107, 5804-5809.  
18983934 G.Dong, and S.S.Golden (2008).
How a cyanobacterium tells time.
  Curr Opin Microbiol, 11, 541-546.  
18846291 R.Narikawa, T.Kohchi, and M.Ikeuchi (2008).
Characterization of the photoactive GAF domain of the CikA homolog (SyCikA, Slr1969) of the cyanobacterium Synechocystis sp. PCC 6803.
  Photochem Photobiol Sci, 7, 1253-1259.  
18344369 S.R.Mackey, J.S.Choi, Y.Kitayama, H.Iwasaki, G.Dong, and S.S.Golden (2008).
Proteins found in a CikA interaction assay link the circadian clock, metabolism, and cell division in Synechococcus elongatus.
  J Bacteriol, 190, 3738-3746.  
17804240 S.R.Mackey, and S.S.Golden (2007).
Winding up the cyanobacterial circadian clock.
  Trends Microbiol, 15, 381-388.  
18419290 S.S.Golden (2007).
Integrating the circadian oscillator into the life of the cyanobacterial cell.
  Cold Spring Harb Symp Quant Biol, 72, 331-338.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.