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7Z5F

VP2-only capsid of MVM D263A mutant

This is a non-PDB format compatible entry.
Summary for 7Z5F
Entry DOI10.2210/pdb7z5f/pdb
EMDB information14521
DescriptorCapsid protein VP1 (1 entity in total)
Functional Keywordscapsid, mvm, vlp, virus like particle
Biological sourceMinute virus of mice
Total number of polymer chains1
Total formula weight64526.38
Authors
Luque, D.,Ortega-Esteban, A.,Valbuena, A.,Vilas, J.L.,Rodriguez-Huete, A.,Mateu, M.G.,Caston, J.R. (deposition date: 2022-03-09, release date: 2023-03-08, Last modification date: 2024-07-17)
Primary citationLuque, D.,Ortega-Esteban, A.,Valbuena, A.,Luis Vilas, J.,Rodriguez-Huete, A.,Mateu, M.G.,Caston, J.R.
Equilibrium Dynamics of a Biomolecular Complex Analyzed at Single-amino Acid Resolution by Cryo-electron Microscopy.
J.Mol.Biol., 435:168024-168024, 2023
Cited by
PubMed Abstract: 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.
PubMed: 36828271
DOI: 10.1016/j.jmb.2023.168024
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.22 Å)
Structure validation

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数据于2025-08-27公开中

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