期刊
PROTEIN SCIENCE
卷 16, 期 3, 页码 465-475出版社
WILEY
DOI: 10.1110/ps.062532007
关键词
protein structure/folding; enzymes; heteronuclear NMR; circadian clock; cyanobacteria; histidine protein kinase; metabolism; photosynthesis; pseudo-receiver
资金
- NIGMS NIH HHS [R01 GM062419, GM62419, R56 GM064576, R01 GM064576, GM064576] Funding Source: Medline
- NINDS NIH HHS [NS39546, P01 NS039546] Funding Source: Medline
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-3methyl-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.
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