View source for 7rvb


==High resolution map of molecular chaperone Artemin==
<StructureSection load='7rvb' size='340' side='right'caption='[[7rvb]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7rvb]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Artemia_franciscana Artemia franciscana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RVB 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]] 2.04&#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=7rvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rvb OCA], [https://pdbe.org/7rvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rvb RCSB], [https://www.ebi.ac.uk/pdbsum/7rvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rvb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8WQM8_ARTSF Q8WQM8_ARTSF] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[RuleBase:RU361145]
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== Publication Abstract from PubMed ==
The protein artemin acts as both an RNA and protein chaperone and constitutes over 10% of all protein in Artemia cysts during diapause. However, its mechanistic details remain elusive since no high-resolution structure of artemin exists. Here we report the full-length structure of artemin at 2.04 A resolution. The cryo-EM map contains density for an intramolecular disulfide bond between Cys22-Cys61 and resolves the entire C-terminus extending into the core of the assembled protein cage but in a different configuration than previously hypothesized with molecular modeling. We also provide data supporting the role of C-terminal helix F towards stabilizing the dimer form that is believed to be important for its chaperoning activity. We were able to destabilize this effect by placing a tag at the C-terminus to fully pack the internal cavity and cause limited steric hindrance.

Cryo-EM structure of the diapause chaperone artemin.,Parvate AD, Powell SM, Brookreson JT, Moser TH, Novikova IV, Zhou M, Evans JE Front Mol Biosci. 2022 Nov 28;9:998562. doi: 10.3389/fmolb.2022.998562. , eCollection 2022. PMID:36518848<ref>PMID:36518848</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7rvb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Artemia franciscana]]
[[Category: Large Structures]]
[[Category: Brookreason JT]]
[[Category: Evans JE]]
[[Category: Novikova IV]]
[[Category: Parvate AD]]
[[Category: Powell SM]]