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NMR structure of the pseudo ‐receiver domain of CikA
Author(s) -
Gao Tiyu,
Zhang Xiaofan,
Ivleva Natalia B.,
Golden Susan S.,
LiWang Andy
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062532007
Subject(s) - domain (mathematical analysis) , hamp domain , protein kinase domain , histidine kinase , chemistry , residue (chemistry) , binding domain , microbiology and biotechnology , histidine , biochemistry , biophysics , biology , binding site , amino acid , mathematics , gene , mathematical analysis , mutant
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.