7z5f
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7z5f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Minute_virus_of_mice Minute virus of mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z5F FirstGlance]. <br> | <table><tr><td colspan='2'>[[7z5f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Minute_virus_of_mice Minute virus of mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z5F FirstGlance]. <br> | ||
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7z5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z5f OCA], [https://pdbe.org/7z5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z5f RCSB], [https://www.ebi.ac.uk/pdbsum/7z5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z5f ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.22Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7z5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z5f OCA], [https://pdbe.org/7z5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z5f RCSB], [https://www.ebi.ac.uk/pdbsum/7z5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z5f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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. | 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. | ||
| - | Equilibrium Dynamics of a Biomolecular Complex Analyzed at Single-amino Acid Resolution by Cryo-electron Microscopy.,Luque D, Ortega-Esteban A, Valbuena A, Luis Vilas J, Rodriguez-Huete A, Mateu MG, Caston JR J Mol Biol. 2023 | + | Equilibrium Dynamics of a Biomolecular Complex Analyzed at Single-amino Acid Resolution by Cryo-electron Microscopy.,Luque D, Ortega-Esteban A, Valbuena A, Luis Vilas J, Rodriguez-Huete A, Mateu MG, Caston JR J Mol Biol. 2023 Apr 15;435(8):168024. doi: 10.1016/j.jmb.2023.168024. Epub 2023 , Feb 23. PMID:36828271<ref>PMID:36828271</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 7z5f" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7z5f" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
VP2-only capsid of MVM D263A mutant
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