The pore structure of the closed RyR1 channel.
Using single particle electron cryomicroscopy, several helices in the membrane-spanning region of RyR1, including an inner transmembrane helix, a short pore helix, and a helix parallel to the membrane on the cytoplasmic side, have been clearly resolved. Our model places a highly conserved glycine (G4934) at the hinge position of the bent inner helix and two rings of negative charges at the luminal and cytoplasmic mouths of the pore. The kinked inner helix closely resembles the inner helix of the open MthK channel, suggesting that kinking alone does not open RyR1, as proposed for K+ channels.
Ludtke
Steven J
SJ
National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
Serysheva
Irina I
II
Hamilton
Susan L
SL
Chiu
Wah
W
D000595:Amino Acid Sequence; D000818:Animals; D020285:Cryoelectron Microscopy; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011817:Rabbits; D019837:Ryanodine Receptor Calcium Release Channel / Q000737:chemistry* / Q000378:metabolism; D040681:Structural Homology, Protein
D019837:Ryanodine Receptor Calcium Release Channel