8X4D
Cryo-EM structure of Ryanodine receptor 1 (TM helix S0,20 uM Ca2+, 2 mM ATP)
This is a non-PDB format compatible entry.
Summary for 8X4D
| Entry DOI | 10.2210/pdb8x4d/pdb |
| EMDB information | 38047 |
| Descriptor | Ryanodine receptor 1, CALCIUM ION, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | ryanodine receptor, calcium release channel, membrane protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 4 |
| Total formula weight | 2265823.54 |
| Authors | |
| Primary citation | Wei, R.,Chen, Q.,Zhang, L.,Liu, C.,Liu, C.,Yin, C.C.,Hu, H. Structural insights into transmembrane helix S0 facilitated RyR1 channel gating by Ca 2+ /ATP. Nat Commun, 16:1936-1936, 2025 Cited by PubMed Abstract: The type-1 ryanodine receptor (RyR1) is an intracellular calcium release channel for skeletal muscle excitation-contraction coupling. Previous structural studies showed that the RyR1 activity is modulated by the exogenous regulators including caffeine, ryanodine, PCB-95 and diamide. An additional transmembrane helix, located adjacent to S1 and S4, has been observed in some structures, although its function remains unclear. Here, we report that using a mild purification procedure, this helix is co-purified with RyR1 and is designated as S0. When RyR1 is coupled with S0, it can be activated by Ca to an open state; however when decoupled from S0, it remains in primed state. S0 regulates the channel conformation by directly affecting the TM domain via the pVSD-S0-S4/S5 linker coupling, which facilitates the dilation of S6. Our results demonstrate that S0 is an essential component of RyR1 and plays a key role in the physiological regulation of RyR1 channel gating. PubMed: 39994184DOI: 10.1038/s41467-025-57074-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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