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TitleStructure of the rabbit ryanodine receptor RyR1 at near-atomic resolution.
Journal, issue, pagesNature, Vol. 517, Issue 7532, Page 50-55, Year 2015
Publish dateJan 1, 2015
AuthorsZhen Yan / Xiaochen Bai / Chuangye Yan / Jianping Wu / Zhangqiang Li / Tian Xie / Wei Peng / Changcheng Yin / Xueming Li / Sjors H W Scheres / Yigong Shi / Nieng Yan /
PubMed AbstractThe 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 ...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.
External linksNature / PubMed:25517095 / PubMed Central
MethodsEM (single particle)
Resolution3.8 Å
Structure data

2807

3j8h

EMDB-2807: Single-particle electron cryo-microscopy structure of ryanodine receptor RyR1 in complex with FKBP12
PDB-3j8h: Structure of the rabbit ryanodine receptor RyR1 in complex with FKBP12 at 3.8 Angstrom resolution
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • oryctolagus cuniculus (rabbit)
KeywordsTRANSPORT PROTEIN/ISOMERASE / rabbit ryanodine receptor RyR1 / high-conductance intracellular Ca2+ channels / excitation-contraction coupling / TRANSPORT PROTEIN-ISOMERASE complex

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