7M6L

High resolution structure of the membrane embedded skeletal muscle ryanodine receptor

This is a non-PDB format compatible entry.

Summary for 7M6L

• Entry DOI: 10.2210/pdb7m6l/pdb
• EMDB information: 23692 23699
• Descriptor: Peptidyl-prolyl cis-trans isomerase FKBP1B, Ryanodine receptor 1, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: ryanodine receptor, calcium, membrane, liposome, membrane protein-isomerase complex, membrane protein/isomerase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 8
• Total formula weight: 2314055.94

Authors

Melville, Z.,Kim, K.,Clarke, O.B.,Marks, A.R. (deposition date: 2021-03-25, release date: 2021-08-18, Last modification date: 2024-11-20)

Primary citation

Melville, Z.,Kim, K.,Clarke, O.B.,Marks, A.R.
High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor.
Structure, 30:172-, 2022

PubMed Abstract: The type 1 ryanodine receptor (RyR)/calcium release channel on the sarcoplasmic reticulum (SR) is required for skeletal muscle excitation-contraction coupling and is the largest known ion channel, composed of four 565-kDa protomers. Cryogenic electron microscopy (cryo-EM) studies of the RyR have primarily used detergent to solubilize the channel; in the present study, we have used cryo-EM to solve high-resolution structures of the channel in liposomes using a gel-filtration approach with on-column detergent removal to form liposomes and incorporate the channel simultaneously. This allowed us to resolve the structure of the channel in the primed and open states at 3.4 and 4.0 Å, respectively, with a single dataset. This method offers validation for detergent-based structures of the RyR and offers a starting point for utilizing a chemical gradient mimicking the SR, where Ca concentrations are millimolar in the lumen and nanomolar in the cytosol.

PubMed: 34469755
DOI: 10.1016/j.str.2021.08.001

Experimental method

ELECTRON MICROSCOPY (3.98 Å)