5H3O

Structure of a eukaryotic cyclic nucleotide-gated channel

Summary for 5H3O

• Entry DOI: 10.2210/pdb5h3o/pdb
• EMDB information: 6656 6657
• Descriptor: Cyclic nucleotide-gated cation channel, CYCLIC GUANOSINE MONOPHOSPHATE, SODIUM ION (3 entities in total)
• Functional Keywords: tax-4, cng, channel, open state, transport protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 4
• Total formula weight: 338673.38

Authors

Li, M.,Zhou, X.,Wang, S.,Michailidis, I.,Gong, Y.,Su, D.,Li, H.,Li, X.,Yang, J. (deposition date: 2016-10-26, release date: 2017-01-25, Last modification date: 2024-05-29)

Primary citation

Li, M.,Zhou, X.,Wang, S.,Michailidis, I.,Gong, Y.,Su, D.,Li, H.,Li, X.,Yang, J.
Structure of a eukaryotic cyclic-nucleotide-gated channel.
Nature, 542:60-65, 2017

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 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.

PubMed: 28099415
DOI: 10.1038/nature20819

Experimental method

ELECTRON MICROSCOPY (3.5 Å)