5J8V

Structure of rabbit ryanodine receptor RyR1 open state activated by calcium ion

Summary for 5J8V

• Entry DOI: 10.2210/pdb5j8v/pdb
• EMDB information: 8073
• Descriptor: Ryanodine receptor 1 (1 entity in total)
• Functional Keywords: endoplasmic reticula, skeletal muscles, intracellular calcium ion channel, activated by calcium ion, transport protein
• Biological source: Oryctolagus cuniculus (Rabbit)
• Total number of polymer chains: 4
• Total formula weight: 2263634.50

Authors

Wang, X.,Wei, R.,Yin, C.,Sun, F. (deposition date: 2016-04-08, release date: 2016-09-14, Last modification date: 2024-11-13)

Primary citation

Wei, R.,Wang, X.,Zhang, Y.,Mukherjee, S.,Zhang, L.,Chen, Q.,Huang, X.,Jing, S.,Liu, C.,Li, S.,Wang, G.,Xu, Y.,Zhu, S.,Williams, A.J.,Sun, F.,Yin, C.C.
Structural insights into Ca(2+)-activated long-range allosteric channel gating of RyR1
Cell Res., 26:977-994, 2016

PubMed Abstract: Ryanodine receptors (RyRs) are a class of giant ion channels with molecular mass over 2.2 mega-Daltons. These channels mediate calcium signaling in a variety of cells. Since more than 80% of the RyR protein is folded into the cytoplasmic assembly and the remaining residues form the transmembrane domain, it has been hypothesized that the activation and regulation of RyR channels occur through an as yet uncharacterized long-range allosteric mechanism. Here we report the characterization of a Ca(2+)-activated open-state RyR1 structure by cryo-electron microscopy. The structure has an overall resolution of 4.9 Å and a resolution of 4.2 Å for the core region. In comparison with the previously determined apo/closed-state structure, we observed long-range allosteric gating of the channel upon Ca(2+) activation. In-depth structural analyses elucidated a novel channel-gating mechanism and a novel ion selectivity mechanism of RyR1. Our work not only provides structural insights into the molecular mechanisms of channel gating and regulation of RyRs, but also sheds light on structural basis for channel-gating and ion selectivity mechanisms for the six-transmembrane-helix cation channel family.

PubMed: 27573175
DOI: 10.1038/cr.2016.99

Experimental method

ELECTRON MICROSCOPY (4.9 Å)