5GL1

Structure of RyR1 in an open state

This is a non-PDB format compatible entry.

Summary for 5GL1

• Entry DOI: 10.2210/pdb5gl1/pdb
• Related: 3J8H 5GKY 5GKZ 5GL0
• EMDB information: 2807 9519 9520 9521
• Descriptor: Ryanodine receptor 1, Peptidyl-prolyl cis-trans isomerase FKBP1A, ZINC ION (3 entities in total)
• Functional Keywords: channel, membrane protein, transport protein-isomerase complex, transport protein/isomerase
• Biological source: Oryctolagus cuniculus (Rabbit); More
• Total number of polymer chains: 8
• Total formula weight: 2311766.96

Authors

Bai, X.C.,Yan, Z.,Wu, J.P.,Yan, N. (deposition date: 2016-07-07, release date: 2016-08-24, Last modification date: 2024-03-27)

Primary citation

Bai, X.C.,Yan, Z.,Wu, J.P.,Li, Z.Q.,Yan, N.
The Central domain of RyR1 is the transducer for long-range allosteric gating of channel opening
Cell Res., 26:995-1006, 2016

PubMed Abstract: The ryanodine receptors (RyRs) are intracellular calcium channels responsible for rapid release of Ca(2+) from the sarcoplasmic/endoplasmic reticulum (SR/ER) to the cytoplasm, which is essential for the excitation-contraction (E-C) coupling of cardiac and skeletal muscles. The near-atomic resolution structure of closed RyR1 revealed the molecular details of this colossal channel, while the long-range allosteric gating mechanism awaits elucidation. Here, we report the cryo-EM structures of rabbit RyR1 in three closed conformations at about 4 Å resolution and an open state at 5.7 Å. Comparison of the closed RyR1 structures shows a breathing motion of the cytoplasmic platform, while the channel domain and its contiguous Central domain remain nearly unchanged. Comparison of the open and closed structures shows a dilation of the S6 tetrahelical bundle at the cytoplasmic gate that leads to channel opening. During the pore opening, the cytoplasmic "O-ring" motif of the channel domain and the U-motif of the Central domain exhibit coupled motion, while the Central domain undergoes domain-wise displacement. These structural analyses provide important insight into the E-C coupling in skeletal muscles and identify the Central domain as the transducer that couples the conformational changes of the cytoplasmic platform to the gating of the central pore.

PubMed: 27468892
DOI: 10.1038/cr.2016.89

Experimental method

ELECTRON MICROSCOPY (5.7 Å)