Structure of a eukaryotic cyclic-nucleotide-gated channel

Minghui Li, Xiaoyuan Zhou, Shu Wang, Ioannis Michailidis, Ye Gong, Deyuan Su, Huan Li, Xueming Li () and Jian Yang ()
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Minghui Li: Columbia University
Xiaoyuan Zhou: Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University
Shu Wang: Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Chinese Academy of Sciences
Ioannis Michailidis: Columbia University
Ye Gong: Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Chinese Academy of Sciences
Deyuan Su: Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Chinese Academy of Sciences
Huan Li: Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Chinese Academy of Sciences
Xueming Li: Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University
Jian Yang: Columbia University

Nature, 2017, vol. 542, issue 7639, 60-65

Abstract: 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.

Date: 2017
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DOI: 10.1038/nature20819

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