2K0G

Solution Structure of a Bacterial Cyclic Nucleotide-Activated K+ Channel Binding Domain in Complex with cAMP

2K0G の概要

• エントリーDOI: 10.2210/pdb2k0g/pdb
• 分子名称: Mll3241 protein, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (2 entities in total)
• 機能のキーワード: membrane protein, ion channel, helical bundle beta barrel core, phosphate binding cassette with camp bound, cyclic nucleotide binding domain, solution structure
• 由来する生物種: Rhizobium loti (Mesorhizobium loti)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: Q98GN8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15312.43

構造登録者

Schunke, S.,Stoldt, M.,Willbold, D. (登録日: 2008-02-02, 公開日: 2009-02-10, 最終更新日: 2024-05-29)

主引用文献

Schunke, S.,Stoldt, M.,Novak, K.,Kaupp, U.B.,Willbold, D.
Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP.
Embo Rep., 10:729-735, 2009

PubMed Abstract: Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are crucial in neuronal excitability and signal transduction of sensory cells. HCN and CNG channels are activated by binding of cyclic nucleotides to their intracellular cyclic nucleotide-binding domain (CNBD). However, the mechanism by which the binding of cyclic nucleotides opens these channels is not well understood. Here, we report the solution structure of the isolated CNBD of a cyclic nucleotide-sensitive K(+) channel from Mesorhizobium loti. The protein consists of a wide anti-parallel beta-roll topped by a helical bundle comprising five alpha-helices and a short 3(10)-helix. In contrast to the dimeric arrangement ('dimer-of-dimers') in the crystal structure, the solution structure clearly shows a monomeric fold. The monomeric structure of the CNBD supports the hypothesis that the CNBDs transmit the binding signal to the channel pore independently of each other.

PubMed: 19465888
DOI: 10.1038/embor.2009.68

実験手法

SOLUTION NMR