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| Title | Structure of a eukaryotic cyclic-nucleotide-gated channel. |
|---|---|
| Journal, issue, pages | Nature, Vol. 542, Issue 7639, Page 60-65, Year 2017 |
| Publish date | Feb 2, 2017 |
 Authors | Minghui Li / Xiaoyuan Zhou / Shu Wang / Ioannis Michailidis / Ye Gong / Deyuan Su / Huan Li / Xueming Li / Jian Yang /   |
| PubMed Abstract | Cyclic-nucleotide-gated channels are essential for vision and olfaction. They belong to the voltage-gated ion channel superfamily but their activities are controlled by intracellular cyclic ...Cyclic-nucleotide-gated channels are essential for vision and olfaction. They belong to the voltage-gated ion channel superfamily but their activities are controlled by intracellular cyclic nucleotides instead of transmembrane voltage. Here we report a 3.5-Å-resolution single-particle electron cryo-microscopy structure of a cyclic-nucleotide-gated channel from Caenorhabditis elegans in the cyclic guanosine monophosphate (cGMP)-bound open state. The channel has an unusual voltage-sensor-like domain, accounting for its deficient voltage dependence. A carboxy-terminal linker connecting S6 and the cyclic-nucleotide-binding domain interacts directly with both the voltage-sensor-like domain and the pore domain, forming a gating ring that couples conformational changes triggered by cyclic nucleotide binding to the gate. The selectivity filter is lined by the carboxylate side chains of a functionally important glutamate and three rings of backbone carbonyls. This structure provides a new framework for understanding mechanisms of ion permeation, gating and channelopathy of cyclic-nucleotide-gated channels and cyclic nucleotide modulation of related channels. |
 External links | Nature / PubMed:28099415 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.5 - 4.5 Å |
| Structure data | EMDB-6656, PDB-5h3o:  EMDB-6657: |
| Chemicals |  ChemComp-PCG:  ChemComp-NA: |
| Source |
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 Keywords |  TRANSPORT PROTEIN / TAX-4 / CNG / Channel / Open state |
