2j48
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(New page: 200px<br /><applet load="2j48" size="350" color="white" frame="true" align="right" spinBox="true" caption="2j48" /> '''NMR STRUCTURE OF THE PSEUDO-RECEIVER DOMAIN ...)
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Revision as of 18:50, 29 January 2008
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NMR STRUCTURE OF THE PSEUDO-RECEIVER DOMAIN OF THE CIKA PROTEIN.
Overview
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.
About this Structure
2J48 is a Single protein structure of sequence from Synechococcus elongatus. Active as Histidine kinase, with EC number 2.7.13.3 Full crystallographic information is available from OCA.
Reference
NMR structure of the pseudo-receiver domain of CikA., Gao T, Zhang X, Ivleva NB, Golden SS, LiWang A, Protein Sci. 2007 Mar;16(3):465-75. PMID:17322531
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