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TitleRetrieving functional pathways of biomolecules from single-particle snapshots.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 4734, Year 2020
Publish dateSep 18, 2020
AuthorsAli Dashti / Ghoncheh Mashayekhi / Mrinal Shekhar / Danya Ben Hail / Salah Salah / Peter Schwander / Amedee des Georges / Abhishek Singharoy / Joachim Frank / Abbas Ourmazd /
PubMed AbstractA 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 ...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.
External linksNat Commun / PubMed:32948759 / PubMed Central
MethodsEM (single particle)
Resolution4.5 Å
Structure data

20486

6pv6

EMDB-20486, PDB-6pv6:
Functional Pathways of Biomolecules Retrieved from Single-particle Snapshots
Method: EM (single particle) / Resolution: 4.5 Å

22392

7jmf

EMDB-22392, PDB-7jmf:
Functional Pathways of Biomolecules Retrieved from Single-particle Snapshots - Frame 42 - State 6 (S6)
Method: EM (single particle) / Resolution: 4.5 Å

22393

7jmg

EMDB-22393, PDB-7jmg:
Functional Pathways of Biomolecules Retrieved from Single-particle Snapshots - Frame 22 - State 2 (S2)
Method: EM (single particle) / Resolution: 4.5 Å

22394

7jmh

EMDB-22394, PDB-7jmh:
Functional Pathways of Biomolecules Retrieved from Single-particle Snapshots - Frame 35 - State 4 (S4)
Method: EM (single particle) / Resolution: 4.5 Å

22395

7jmi

EMDB-22395, PDB-7jmi:
Functional Pathways of Biomolecules Retrieved from Single-particle Snapshots - Frame 29 - State 3 (S3)
Method: EM (single particle) / Resolution: 4.5 Å

22396

7jmj

EMDB-22396, PDB-7jmj:
Functional Pathways of Biomolecules Retrieved from Single-particle Snapshots - Frame 37 - State 5 (S5)
Method: EM (single particle) / Resolution: 4.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

Source
  • oryctolagus cuniculus (rabbit)
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ion channel / Ca2+ channel / excitation/contraction coupling

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