3J8H
Structure of the rabbit ryanodine receptor RyR1 in complex with FKBP12 at 3.8 Angstrom resolution
This is a non-PDB format compatible entry.
Summary for 3J8H
Entry DOI | 10.2210/pdb3j8h/pdb |
EMDB information | 2807 |
Descriptor | Ryanodine receptor 1, Peptidyl-prolyl cis-trans isomerase FKBP1A, ZINC ION (3 entities in total) |
Functional Keywords | rabbit ryanodine receptor ryr1, high-conductance intracellular ca2+ channels, excitation-contraction coupling, transport protein-isomerase complex, transport protein/isomerase |
Biological source | Oryctolagus cuniculus (rabbit) More |
Total number of polymer chains | 8 |
Total formula weight | 2048453.92 |
Authors | |
Primary citation | Yan, Z.,Bai, X.C.,Yan, C.,Wu, J.,Li, Z.,Xie, T.,Peng, W.,Yin, C.C.,Li, X.,Scheres, S.H.,Shi, Y.,Yan, N. Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution. Nature, 517:50-55, 2015 Cited by PubMed Abstract: The ryanodine receptors (RyRs) are high-conductance intracellular Ca(2+) channels that play a pivotal role in the excitation-contraction coupling of skeletal and cardiac muscles. RyRs are the largest known ion channels, with a homotetrameric organization and approximately 5,000 residues in each protomer. Here we report the structure of the rabbit RyR1 in complex with its modulator FKBP12 at an overall resolution of 3.8 Å, determined by single-particle electron cryomicroscopy. Three previously uncharacterized domains, named central, handle and helical domains, display the armadillo repeat fold. These domains, together with the amino-terminal domain, constitute a network of superhelical scaffold for binding and propagation of conformational changes. The channel domain exhibits the voltage-gated ion channel superfamily fold with distinct features. A negative-charge-enriched hairpin loop connecting S5 and the pore helix is positioned above the entrance to the selectivity-filter vestibule. The four elongated S6 segments form a right-handed helical bundle that closes the pore at the cytoplasmic border of the membrane. Allosteric regulation of the pore by the cytoplasmic domains is mediated through extensive interactions between the central domains and the channel domain. These structural features explain high ion conductance by RyRs and the long-range allosteric regulation of channel activities. PubMed: 25517095DOI: 10.1038/nature14063 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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