7odw: Difference between revisions

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'''Unreleased structure'''


The entry 7odw is ON HOLD  until Paper Publication
==Model of Haliangium ochraceum encapsulin from icosahedral single particle reconstruction==
<StructureSection load='7odw' size='340' side='right'caption='[[7odw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ODW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ODW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.5&#8491;</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=7odw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7odw OCA], [https://pdbe.org/7odw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7odw RCSB], [https://www.ebi.ac.uk/pdbsum/7odw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7odw ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Encapsulins are protein nanocompartments that house various cargo enzymes, including a family of decameric ferritin-like proteins. Here, we study a recombinant Haliangium ochraceum encapsulin:encapsulated ferritin complex using cryo-electron microscopy and hydrogen/deuterium exchange mass spectrometry to gain insight into the structural relationship between the encapsulin shell and its protein cargo. An asymmetric single-particle reconstruction reveals four encapsulated ferritin decamers in a tetrahedral arrangement within the encapsulin nanocompartment. This leads to a symmetry mismatch between the protein cargo and the icosahedral encapsulin shell. The encapsulated ferritin decamers are offset from the interior face of the encapsulin shell. Using hydrogen/deuterium exchange mass spectrometry, we observed the dynamic behavior of the major fivefold pore in the encapsulin shell and show the pore opening via the movement of the encapsulin A-domain. These data will accelerate efforts to engineer the encapsulation of heterologous cargo proteins and to alter the permeability of the encapsulin shell via pore modifications.


Authors: Marles-Wright, J., Basle, A., Clarke, D.J., Ross, J.
Pore dynamics and asymmetric cargo loading in an encapsulin nanocompartment.,Ross J, McIver Z, Lambert T, Piergentili C, Bird JE, Gallagher KJ, Cruickshank FL, James P, Zarazua-Arvizu E, Horsfall LE, Waldron KJ, Wilson MD, Mackay CL, Basle A, Clarke DJ, Marles-Wright J Sci Adv. 2022 Jan 28;8(4):eabj4461. doi: 10.1126/sciadv.abj4461. Epub 2022 Jan, 26. PMID:35080974<ref>PMID:35080974</ref>


Description: Model of Haliangium ochraceum encapsulin from icosahedral single particle reconstruction
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Ross, J]]
<div class="pdbe-citations 7odw" style="background-color:#fffaf0;"></div>
[[Category: Marles-Wright, J]]
== References ==
[[Category: Clarke, D.J]]
<references/>
[[Category: Basle, A]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Basle A]]
[[Category: Clarke DJ]]
[[Category: Marles-Wright J]]
[[Category: Ross J]]
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