6CJT

Structure of the SthK cyclic nucleotide-gated potassium channel in complex with cGMP

6CJT の概要

• エントリーDOI: 10.2210/pdb6cjt/pdb
• EMDBエントリー: 7482 7483 7484
• 分子名称: SthK cyclic nucleotide-gated potassium channel, CYCLIC GUANOSINE MONOPHOSPHATE, (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate (3 entities in total)
• 機能のキーワード: ion channel, tetramer, lipid, cgmp, transport protein
• 由来する生物種: Spirochaeta thermophila
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 223831.28

構造登録者

Nimigean, C.M.,Rheinberger, J. (登録日: 2018-02-26, 公開日: 2018-08-01, 最終更新日: 2024-03-13)

主引用文献

Rheinberger, J.,Gao, X.,Schmidpeter, P.A.,Nimigean, C.M.
Ligand discrimination and gating in cyclic nucleotide-gated ion channels from apo and partial agonist-bound cryo-EM structures.
Elife, 7:-, 2018

PubMed Abstract: Cyclic nucleotide-modulated channels have important roles in visual signal transduction and pacemaking. Binding of cyclic nucleotides (cAMP/cGMP) elicits diverse functional responses in different channels within the family despite their high sequence and structure homology. The molecular mechanisms responsible for ligand discrimination and gating are unknown due to lack of correspondence between structural information and functional states. Using single particle cryo-electron microscopy and single-channel recording, we assigned functional states to high-resolution structures of SthK, a prokaryotic cyclic nucleotide-gated channel. The structures for apo, cAMP-bound, and cGMP-bound SthK in lipid nanodiscs, correspond to no, moderate, and low single-channel activity, respectively, consistent with the observation that all structures are in resting, closed states. The similarity between apo and ligand-bound structures indicates that ligand-binding domains are strongly coupled to pore and SthK gates in an allosteric, concerted fashion. The different orientations of cAMP and cGMP in the 'resting' and 'activated' structures suggest a mechanism for ligand discrimination.

PubMed: 30028291
DOI: 10.7554/eLife.39775

実験手法

ELECTRON MICROSCOPY (3.46 Å)