Single-particle electron cryomicroscopy revealed the structural basis for the gating mechanism of the porcine heart type 2 ryanodine receptor (RyR2) in both open and closed states.
Near-atomic resolution structures of porcine heart RyR2 in open and closed states provide important insights into its gating and disease mechanisms.
from the sarco(endo)plasmic reticulum of a variety of cells. Here, we report the structures of RyR2 from porcine heart in both the open and closed states at near-atomic resolutions determined using single-particle electron cryomicroscopy. Structural comparison reveals a breathing motion of the overall cytoplasmic region resulted from the interdomain movements of amino-terminal domains (NTDs), Helical domains, and Handle domains, whereas almost no intradomain shifts are observed in these armadillo repeats-containing domains. Outward rotations of the Central domains, which integrate the conformational changes of the cytoplasmic region, lead to the dilation of the cytoplasmic gate through coupled motions. Our structural and mutational characterizations provide important insights into the gating and disease mechanism of RyRs.
Peng et al. (2016) studied this question. Single-particle electron cryomicroscopy revealed the structural basis for the gating mechanism of the porcine heart type 2 ryanodine receptor (RyR2) in both open and closed states.