7TDI
Rabbit RyR1 with AMP-PCP and high Ca2+ embedded in nanodisc in closed-inactivated conformation class 2 (Dataset-A)
This is a non-PDB format compatible entry.
Summary for 7TDI
| Entry DOI | 10.2210/pdb7tdi/pdb |
| Related | 7K09 7K0T 7TDG 7TDH 7TDK |
| EMDB information | 25830 25833 |
| Descriptor | Ryanodine receptor 1,Ryanodine receptor 1,RyR1, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ZINC ION, ... (4 entities in total) |
| Functional Keywords | ryanodine receptor, ryr1, intracellular calcium channel, ca2+, inactivation, excitation-contraction coupling, transport protein |
| Biological source | Oryctolagus cuniculus (rabbit) More |
| Total number of polymer chains | 4 |
| Total formula weight | 2137256.09 |
| Authors | Nayak, A.R.,Samso, M. (deposition date: 2021-12-31, release date: 2022-03-09, Last modification date: 2024-11-13) |
| Primary citation | Nayak, A.R.,Samso, M. Ca 2+ -inactivation of the mammalian ryanodine receptor type 1 in a lipidic environment revealed by cryo-EM. Elife, 11:-, 2022 Cited by PubMed Abstract: Activation of the intracellular Ca channel ryanodine receptor (RyR) triggers a cytosolic Ca surge, while elevated cytosolic Ca inhibits the channel in a negative feedback mechanism. Cryogenic electron microscopy of rabbit RyR1 embedded in nanodiscs under partially inactivating Ca conditions revealed an open and a closed-inactivated conformation. Ca binding to the high-affinity site engages the central and C-terminal domains into a block, which pries the S6 four-helix bundle open. Further rotation of this block pushes S6 toward the central axis, closing (inactivating) the channel. Main characteristics of the Ca-inactivated conformation are downward conformation of the cytoplasmic assembly and tightly knit subunit interface contributed by a fully occupied Ca activation site, two inter-subunit resolved lipids, and two salt bridges between the EF hand domain and the S2-S3 loop validated by disease-causing mutations. The structural insight illustrates the prior Ca activation prerequisite for Ca inactivation and provides for a seamless transition from inactivated to closed conformations. PubMed: 35257661DOI: 10.7554/eLife.75568 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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