7JMJ
Functional Pathways of Biomolecules Retrieved from Single-particle Snapshots - Frame 37 - State 5 (S5)
This is a non-PDB format compatible entry.
Summary for 7JMJ
| Entry DOI | 10.2210/pdb7jmj/pdb |
| Related | 6PV6 7JMF 7JMG 7JMH 7JMI |
| EMDB information | 20486 22392 22393 22394 22395 22396 |
| Descriptor | Peptidyl-prolyl cis-trans isomerase FKBP1B, ryanodine receptor type 1, ZINC ION, ... (4 entities in total) |
| Functional Keywords | ion channel, ca2+ channel, excitation/contraction coupling, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 2056078.04 |
| Authors | Dashti, A.,des Georges, A.,Frank, J.,Ourmazd, A. (deposition date: 2020-07-31, release date: 2020-08-12, Last modification date: 2024-03-06) |
| Primary citation | Dashti, A.,Mashayekhi, G.,Shekhar, M.,Ben Hail, D.,Salah, S.,Schwander, P.,des Georges, A.,Singharoy, A.,Frank, J.,Ourmazd, A. Retrieving functional pathways of biomolecules from single-particle snapshots. Nat Commun, 11:4734-4734, 2020 Cited by PubMed Abstract: A primary reason for the intense interest in structural biology is the fact that knowledge of structure can elucidate macromolecular functions in living organisms. Sustained effort has resulted in an impressive arsenal of tools for determining the static structures. But under physiological conditions, macromolecules undergo continuous conformational changes, a subset of which are functionally important. Techniques for capturing the continuous conformational changes underlying function are essential for further progress. Here, we present chemically-detailed conformational movies of biological function, extracted data-analytically from experimental single-particle cryo-electron microscopy (cryo-EM) snapshots of ryanodine receptor type 1 (RyR1), a calcium-activated calcium channel engaged in the binding of ligands. The functional motions differ substantially from those inferred from static structures in the nature of conformationally active structural domains, the sequence and extent of conformational motions, and the way allosteric signals are transduced within and between domains. Our approach highlights the importance of combining experiment, advanced data analysis, and molecular simulations. PubMed: 32948759DOI: 10.1038/s41467-020-18403-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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