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TitleStructural insights into Ca(2+)-activated long-range allosteric channel gating of RyR1.
Journal, issue, pagesCell Res, Vol. 26, Issue 9, Page 977-994, Year 2016
Publish dateAug 30, 2016
AuthorsRisheng Wei / Xue Wang / Yan Zhang / Saptarshi Mukherjee / Lei Zhang / Qiang Chen / Xinrui Huang / Shan Jing / Congcong Liu / Shuang Li / Guangyu Wang / Yaofang Xu / Sujie Zhu / Alan J Williams / Fei Sun / Chang-Cheng Yin /
PubMed AbstractRyanodine receptors (RyRs) are a class of giant ion channels with molecular mass over 2.2 mega-Daltons. These channels mediate calcium signaling in a variety of cells. Since more than 80% of the RyR ...Ryanodine receptors (RyRs) are a class of giant ion channels with molecular mass over 2.2 mega-Daltons. These channels mediate calcium signaling in a variety of cells. Since more than 80% of the RyR protein is folded into the cytoplasmic assembly and the remaining residues form the transmembrane domain, it has been hypothesized that the activation and regulation of RyR channels occur through an as yet uncharacterized long-range allosteric mechanism. Here we report the characterization of a Ca(2+)-activated open-state RyR1 structure by cryo-electron microscopy. The structure has an overall resolution of 4.9 Å and a resolution of 4.2 Å for the core region. In comparison with the previously determined apo/closed-state structure, we observed long-range allosteric gating of the channel upon Ca(2+) activation. In-depth structural analyses elucidated a novel channel-gating mechanism and a novel ion selectivity mechanism of RyR1. Our work not only provides structural insights into the molecular mechanisms of channel gating and regulation of RyRs, but also sheds light on structural basis for channel-gating and ion selectivity mechanisms for the six-transmembrane-helix cation channel family.
External linksCell Res / PubMed:27573175 / PubMed Central
MethodsEM (single particle)
Resolution4.2 - 7.7 Å
Structure data

8073

5j8v

EMDB-8073: Structure of open state rabbit ryanodine receptor 1 activated by calcium ion
PDB-5j8v: Structure of rabbit ryanodine receptor RyR1 open state activated by calcium ion
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-8074:
Core region of open state rabbit ryanodine receptor 1 activated by calcium ion
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-8171:
Structure of shut state rabbit ryanodine receptor 1 activated by calcium ion
Method: EM (single particle) / Resolution: 7.7 Å

EMDB-8172:
Core region of shut state rabbit ryanodine receptor 1 activated by calcium ion
Method: EM (single particle) / Resolution: 4.9 Å

Source
  • oryctolagus cuniculus (rabbit)
  • Rabbit (rabbit)
KeywordsTRANSPORT PROTEIN / endoplasmic reticula / skeletal muscles / intracellular calcium ion channel / activated by calcium ion

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