5TA3
Structure of rabbit RyR1 (Caffeine/ATP/Ca2+ dataset, class 2)
This is a non-PDB format compatible entry.
Summary for 5TA3
| Entry DOI | 10.2210/pdb5ta3/pdb |
| Related | 5T15 5T9M 5T9N 5T9R 5T9S 5T9V 5TAL 5TAM 5TAN 5TAP 5TAQ 5TAS 5TAT 5TAU 5TAV 5TAW 5TAX 5TAY 5TAZ 5TB0 5TB1 5TB2 5TB3 5TB4 |
| EMDB information | 8342 8372 8373 8374 8375 8376 8377 8378 8379 8380 8381 8382 8383 8384 8385 8386 8387 8388 8389 8390 8391 8392 8393 8394 8395 |
| Descriptor | Peptidyl-prolyl cis-trans isomerase FKBP1B, Ryanodine receptor 1, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | ryr, ca2+, ec coupling, gating, transport protein-isomerase complex, transport protein/isomerase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 1950852.32 |
| Authors | Clarke, O.B.,des Georges, A.,Zalk, R.,Marks, A.R.,Hendrickson, W.A.,Frank, J. (deposition date: 2016-09-09, release date: 2016-10-12, Last modification date: 2018-07-18) |
| Primary citation | des Georges, A.,Clarke, O.B.,Zalk, R.,Yuan, Q.,Condon, K.J.,Grassucci, R.A.,Hendrickson, W.A.,Marks, A.R.,Frank, J. Structural Basis for Gating and Activation of RyR1. Cell, 167:145-157.e17, 2016 Cited by PubMed Abstract: The type-1 ryanodine receptor (RyR1) is an intracellular calcium (Ca(2+)) release channel required for skeletal muscle contraction. Here, we present cryo-EM reconstructions of RyR1 in multiple functional states revealing the structural basis of channel gating and ligand-dependent activation. Binding sites for the channel activators Ca(2+), ATP, and caffeine were identified at interdomain interfaces of the C-terminal domain. Either ATP or Ca(2+) alone induces conformational changes in the cytoplasmic assembly ("priming"), without pore dilation. In contrast, in the presence of all three activating ligands, high-resolution reconstructions of open and closed states of RyR1 were obtained from the same sample, enabling analyses of conformational changes associated with gating. Gating involves global conformational changes in the cytosolic assembly accompanied by local changes in the transmembrane domain, which include bending of the S6 transmembrane segment and consequent pore dilation, displacement, and deformation of the S4-S5 linker and conformational changes in the pseudo-voltage-sensor domain. PubMed: 27662087DOI: 10.1016/j.cell.2016.08.075 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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