View source for 6txl


==Crystal structure of thermotoga maritima E65Q Ferritin==
<StructureSection load='6txl' size='340' side='right'caption='[[6txl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6txl]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TXL 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]] 2.099&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6txl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6txl OCA], [https://pdbe.org/6txl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6txl RCSB], [https://www.ebi.ac.uk/pdbsum/6txl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6txl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9X0L2_THEMA Q9X0L2_THEMA] Iron storage protein (By similarity).[RuleBase:RU361145]
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== Publication Abstract from PubMed ==
Cage forming proteins have numerous potential applications in biomedicine and biotechnology, where the iron storage ferritin is a widely used example. However, controlling ferritin cage assembly/disassembly remains challenging, typically requiring extreme conditions incompatible with many desirable cargoes, particularly for more fragile biopharmaceuticals. Recently, a ferritin from the hyperthermophile bacterium Thermotoga maritima (TmFtn) has been shown to have reversible assembly under mild conditions, offering greater potential biocompatibility in terms of cargo access and encapsulation. Like Archeoglobus fulgidus ferritin (AfFtn), TmFtn forms 24mer cages mediated by metal ions (Mg2+). We have solved the crystal structure of the wild type TmFtn and several mutants displaying different assembly/disassembly properties. These data combined with other biophysical studies allow us to suggest candidate interfacial amino acids crucial in controlling assembly. This work deepens our understanding of how these ferritin complexes assemble and is a useful step towards production of triggerable ferritins in which these properties can be finely designed and controlled.

A single residue can modulate nanocage assembly in salt dependent ferritin.,Kumar M, Markiewicz-Mizera J, Janna Olmos JD, Wilk P, Grudnik P, Biela AP, Jemiola-Rzeminska M, Gorecki A, Chakraborti S, Heddle JG Nanoscale. 2021 Jul 15;13(27):11932-11942. doi: 10.1039/d1nr01632f. PMID:34195748<ref>PMID:34195748</ref>

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

==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Chakraborti S]]
[[Category: Grudnik P]]
[[Category: Heddle J]]
[[Category: Kumar M]]
[[Category: Wilk P]]