› 7vmo

Electron Microscopy
3.5Å resolution

Structure of recombinant RyR2 (Ca2+ dataset, class 1, open state)

Released:
DOI: 10.2210/pdb7vmo/pdb
PDB entry 7vmo coloured by chain, front view.
PDB entry 7vmo coloured by chain, side view.
PDB entry 7vmo coloured by chain, top view.
Source organisms:
Primary publication:
Molecular basis for gating of cardiac ryanodine receptor explains the mechanisms for gain- and loss-of function mutations.
Kobayashi T, Tsutsumi A, Kurebayashi N, Saito K, Kodama M, Sakurai T, Kikkawa M, Murayama T, Ogawa H
OpenAccess logo Nat Commun 13 2821 (2022)
PMID: 35595836
Related structures: EMD-33938

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123217 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ryanodine receptor 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 4966 amino acids
Theoretical weight: 533.65 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: E9Q401 (Residues: 1-4966; Coverage: 100%)
Gene name: Ryr2
Sequence domains:
Peptidyl-prolyl cis-trans isomerase FKBP1B Chains: G, H, I, J
Molecule details ›
Chains: G, H, I, J
Length: 176 amino acids
Theoretical weight: 18.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68106 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP12.6, FKBP1B, FKBP1L, FKBP9, OTK4
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.5Å
Relevant EMDB volumes: EMD-33938
Expression systems:
  • Homo sapiens
  • Escherichia coli

Quick links

Citations

1 review citation

Three-dimensional perspective on ryanodine receptor mutations causing skeletal and cardiac muscle-related diseases.
Iyer et al. (2023)
6 other articles

1 mention without citation

Rapid small-scale nanobody-assisted purification of ryanodine receptors for cryo-EM.
Li et al. (2024)