Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 DOI10.2210/pdb3j8h/pdb
EMDB information2807
DescriptorRyanodine receptor 1, Peptidyl-prolyl cis-trans isomerase FKBP1A, ZINC ION (3 entities in total)
Functional Keywordsrabbit ryanodine receptor ryr1, high-conductance intracellular ca2+ channels, excitation-contraction coupling, transport protein-isomerase complex, transport protein/isomerase
Biological sourceOryctolagus cuniculus (rabbit)
More
Total number of polymer chains8
Total formula weight2048453.92
Authors
Yan, Z.,Bai, X.,Yan, C.,Wu, J.,Scheres, S.H.W.,Shi, Y.,Yan, N. (deposition date: 2014-10-26, release date: 2014-12-10, Last modification date: 2024-02-21)
Primary citationYan, 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: 25517095
DOI: 10.1038/nature14063
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon