7oe2
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Model of closed pentamer of the Haliangium ochraceum encapsulin from symmetry expansion of icosahedral single particle reconstruction== |
| - | <StructureSection load='7oe2' size='340' side='right'caption='[[7oe2]]' scene=''> | + | <StructureSection load='7oe2' size='340' side='right'caption='[[7oe2]], [[Resolution|resolution]] 2.40Å' 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= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7oe2]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliangium_ochraceum_DSM_14365 Haliangium ochraceum DSM 14365]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OE2 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=7oe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oe2 OCA], [https://pdbe.org/7oe2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oe2 RCSB], [https://www.ebi.ac.uk/pdbsum/7oe2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oe2 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]] 2.4Å</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=7oe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oe2 OCA], [https://pdbe.org/7oe2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oe2 RCSB], [https://www.ebi.ac.uk/pdbsum/7oe2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oe2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FER_HALO1 FER_HALO1] Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like ferroxidase that converts Fe(2+) to Fe(3+) iron inside the encapsulin nanocompartment (PubMed:30837306, PubMed:35080974). Mineralized Fe(3+) is released to the exterior of the decameric complex for deposition in the encapsulin nanocompartment. In solution the decamer binds 10-15 iron cations; in the encapsulin nanocompartment the decamer can bind up to 48 ions, perhaps via its internal channel, and on its exterior. The cargo-loaded nanocompartment maximally sequesters up to 4150 Fe ions (By similarity).[UniProtKB:Q2RVS1]<ref>PMID:30837306</ref> <ref>PMID:35080974</ref> | ||
| + | <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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7oe2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Haliangium ochraceum DSM 14365]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Basle A]] |
| + | [[Category: Clarke DJ]] | ||
| + | [[Category: Marles-Wright J]] | ||
| + | [[Category: Ross J]] | ||
Current revision
Model of closed pentamer of the Haliangium ochraceum encapsulin from symmetry expansion of icosahedral single particle reconstruction
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