Structure of a Eukaryotic Cyclic-nucleotide-gated Channel

author:	Li M, Zhou X, Wang S, Michailidis I, Gong Y, Su D, Li H, Li X, Yang J
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 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.
Contact the author:	jianyang@mail.kiz.ac.cn
Page number:	60-65
Issue:	7639
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PubYear:	2017
Volume:	542
Unit code:	152453
Publication name:	Nature
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Paper source:	http://www.nature.com/nature/journal/vaop/ncurrent/pdf/nature20819.pdf
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