5GOA

Cryo-EM structure of RyR2 in open state

This is a non-PDB format compatible entry.

Summary for 5GOA

• Entry DOI: 10.2210/pdb5goa/pdb
• Related: 5GO9
• EMDB information: 9529
• Descriptor: RyR2, ZINC ION (2 entities in total)
• Functional Keywords: membrane protein; channel, transport protein
• Biological source: Sus scrofa (pig)
• Total number of polymer chains: 4
• Total formula weight: 2259884.14

Authors

Peng, W.,Wu, J.P.,Yan, N. (deposition date: 2016-07-26, release date: 2016-10-05, Last modification date: 2024-03-27)

Primary citation

Peng, W.,Shen, H.,Wu, J.P.,Guo, W.,Pan, X.,Wang, R.,Chen, S.R.W.,Yan, N.
Structural basis for the gating mechanism of the type 2 ryanodine receptor RyR2
Science, 354:-, 2016

PubMed Abstract: RyR2 is a high-conductance intracellular calcium (Ca) channel that controls the release of Ca from the sarco(endo)plasmic reticulum of a variety of cells. Here, we report the structures of RyR2 from porcine heart in both the open and closed states at near-atomic resolutions determined using single-particle electron cryomicroscopy. Structural comparison reveals a breathing motion of the overall cytoplasmic region resulted from the interdomain movements of amino-terminal domains (NTDs), Helical domains, and Handle domains, whereas almost no intradomain shifts are observed in these armadillo repeats-containing domains. Outward rotations of the Central domains, which integrate the conformational changes of the cytoplasmic region, lead to the dilation of the cytoplasmic gate through coupled motions. Our structural and mutational characterizations provide important insights into the gating and disease mechanism of RyRs.

PubMed: 27708056
DOI: 10.1126/science.aah5324

Experimental method

ELECTRON MICROSCOPY (4.2 Å)