View source for 6l58


==Cu(II) loaded Tegillarca granosa M-ferritin soaked with Fe(II)==
<StructureSection load='6l58' size='340' side='right'caption='[[6l58]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6l58]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Tegillarca_granosa Tegillarca granosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L58 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9027097&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></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=6l58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l58 OCA], [https://pdbe.org/6l58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l58 RCSB], [https://www.ebi.ac.uk/pdbsum/6l58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l58 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D3JCC5_TEGGR D3JCC5_TEGGR] 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 ==
In addition to its role as an iron storage protein, ferritin can function as a major detoxification component in the innate immune defense, and Cu(2+) ions can also play crucial antibacterial roles in the blood clam, Tegillarca granosa. However, the mechanism of interaction between iron and copper in recombinant Tegillarca granosa ferritin (TgFer) remains to be investigated. In this study, we investigated the crystal structure of TgFer and examined the effects of Fe(2+) and Cu(2+) ions on the TgFer structure and catalytic activity. The crystal structure revealed that TgFer presented a typically 4-3-2 symmetry in a cage-like, spherical shell composed of 24 identical subunits, featuring highly conserved organization in both the ferroxidase center and the 3-fold channel. Structural and biochemical analyses indicated that the 4-fold channel of TgFer could be serviced as potential binding sites of metal ions. Cu(2+) ions appear to bind preferentially with the 3-fold channel as well as ferroxidase site over Fe(2+) ions, possibly inhibiting the ferroxidase activity of TgFer. Our results present a structural and functional characterization of TgFer, providing mechanistic insight into the interactions between TgFer and both Fe(2+) and Cu(2+) ions.

Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa.,Ming T, Jiang Q, Huo C, Huan H, Wu Y, Su C, Qiu X, Lu C, Zhou J, Li Y, Han J, Zhang Z, Su X Front Mol Biosci. 2022 Mar 11;9:800008. doi: 10.3389/fmolb.2022.800008., eCollection 2022. PMID:35359603<ref>PMID:35359603</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6l58" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tegillarca granosa]]
[[Category: Huan HS]]
[[Category: Jiang QQ]]
[[Category: Ming TH]]
[[Category: Su XR]]