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7pkz

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Current revision (12:33, 17 July 2024) (edit) (undo)
 
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==Vault structure in committed conformation==
==Vault structure in committed conformation==
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<StructureSection load='7pkz' size='340' side='right'caption='[[7pkz]]' scene=''>
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<StructureSection load='7pkz' size='340' side='right'caption='[[7pkz]], [[Resolution|resolution]] 9.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PKZ FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PKZ FirstGlance]. <br>
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</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=7pkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pkz OCA], [https://pdbe.org/7pkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pkz RCSB], [https://www.ebi.ac.uk/pdbsum/7pkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pkz ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7pkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pkz OCA], [https://pdbe.org/7pkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pkz RCSB], [https://www.ebi.ac.uk/pdbsum/7pkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pkz ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vaults are ubiquitous ribonucleoprotein particles involved in a diversity of cellular processes, with promising applications as nanodevices for delivery of multiple cargos. The vault shell is assembled by the symmetrical association of multiple copies of the major vault protein that, initially, generates half vaults. The pairwise, anti-parallel association of two half vaults produces whole vaults. Here, using a combination of vault recombinant reconstitution and structural techniques, we characterized the molecular determinants for the vault opening process. This process commences with a relaxation of the vault waist, causing the expansion of the inner cavity. Then, local disengagement of amino-terminal domains at the vault midsection seeds a conformational change that leads to the aperture, facilitating access to the inner cavity where cargo is hosted. These results inform a hitherto uncharacterized step of the vault cycle and will aid current engineering efforts leveraging vault for tailored cargo delivery.
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Symmetry disruption commits vault particles to disassembly.,Guerra P, Gonzalez-Alamos M, Llauro A, Casanas A, Querol-Audi J, de Pablo PJ, Verdaguer N Sci Adv. 2022 Feb 11;8(6):eabj7795. doi: 10.1126/sciadv.abj7795. Epub 2022 Feb 9. PMID:35138889<ref>PMID:35138889</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7pkz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

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Vault structure in committed conformation

PDB ID 7pkz

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