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TitleEquilibrium Dynamics of a Biomolecular Complex Analyzed at Single-amino Acid Resolution by Cryo-electron Microscopy.
Journal, issue, pagesJ Mol Biol, Vol. 435, Issue 8, Page 168024, Year 2023
Publish dateApr 15, 2023
AuthorsDaniel Luque / Alvaro Ortega-Esteban / Alejandro Valbuena / Jose Luis Vilas / Alicia Rodríguez-Huete / Mauricio G Mateu / José R Castón /
PubMed AbstractThe biological function of macromolecular complexes depends not only on large-scale transitions between conformations, but also on small-scale conformational fluctuations at equilibrium. Information ...The biological function of macromolecular complexes depends not only on large-scale transitions between conformations, but also on small-scale conformational fluctuations at equilibrium. Information on the equilibrium dynamics of biomolecular complexes could, in principle, be obtained from local resolution (LR) data in cryo-electron microscopy (cryo-EM) maps. However, this possibility had not been validated by comparing, for a same biomolecular complex, LR data with quantitative information on equilibrium dynamics obtained by an established solution technique. In this study we determined the cryo-EM structure of the minute virus of mice (MVM) capsid as a model biomolecular complex. The LR values obtained correlated with crystallographic B factors and with hydrogen/deuterium exchange (HDX) rates obtained by mass spectrometry (HDX-MS), a gold standard for determining equilibrium dynamics in solution. This result validated a LR-based cryo-EM approach to investigate, with high spatial resolution, the equilibrium dynamics of biomolecular complexes. As an application of this approach, we determined the cryo-EM structure of two mutant MVM capsids and compared their equilibrium dynamics with that of the wild-type MVM capsid. The results supported a previously suggested linkage between mechanical stiffening and impaired equilibrium dynamics of a virus particle. Cryo-EM is emerging as a powerful approach for simultaneously acquiring information on the atomic structure and local equilibrium dynamics of biomolecular complexes.
External linksJ Mol Biol / PubMed:36828271
MethodsEM (single particle)
Resolution3.22 - 3.42 Å
Structure data

14519

7z5d

EMDB-14519, PDB-7z5d:
VP2-only capsid of wt MVM prototype strain p
Method: EM (single particle) / Resolution: 3.42 Å

14520

7z5e

EMDB-14520, PDB-7z5e:
VP2-only capsid of MVM D263A mutant
Method: EM (single particle) / Resolution: 3.32 Å

14521

7z5f

EMDB-14521: VP2-only capsid of wt MVM prototype strain p
PDB-7z5f: VP2-only capsid of MVM D263A mutant
Method: EM (single particle) / Resolution: 3.22 Å

Source
  • minute virus of mice
KeywordsVIRUS LIKE PARTICLE / Capsid / MVM / VLP

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