2J48

NMR structure of the pseudo-receiver domain of the CikA protein.

2J48 の概要

• エントリーDOI: 10.2210/pdb2j48/pdb
• NMR情報: BMRB: 6438
• 分子名称: TWO-COMPONENT SENSOR KINASE (1 entity in total)
• 機能のキーワード: kinase, pseudo-receiver, circadian clock, transferase, response regulator, histidine protein kinase
• 由来する生物種: SYNECHOCOCCUS ELONGATUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12884.99

構造登録者

Gao, T.,Zhang, X.,Golden, S.S.,LiWang, A. (登録日: 2006-08-26, 公開日: 2007-03-06, 最終更新日: 2024-05-15)

主引用文献

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

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: 17322531
DOI: 10.1110/ps.062532007

実験手法

SOLUTION NMR