7cpc: Difference between revisions
New page: '''Unreleased structure''' The entry 7cpc is ON HOLD Authors: Description: Category: Unreleased Structures |
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==His-Mediated Reversible Self-assembly of Ferritin Nanocage with Ni binding== | |||
<StructureSection load='7cpc' size='340' side='right'caption='[[7cpc]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7cpc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Penaeus_japonicus Penaeus japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CPC 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]] 2.801Å</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=NI:NICKEL+(II)+ION'>NI</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=7cpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cpc OCA], [https://pdbe.org/7cpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cpc RCSB], [https://www.ebi.ac.uk/pdbsum/7cpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cpc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/T2B7E1_PENJP T2B7E1_PENJP] 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] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein nanocages represent a class of nanovehicles for a variety of applications. However, precise manipulation of self-assembly behavior of these protein nanocages in response to multiple external stimuli for custom-tailored applications remains challenging. Herein, we established a simple but effective strategy for controlling protein nanocage self-assembly that combines a dual property of His motifs (their significantly pH-dependent protonation state and their capacity to coordinate with transition metals) with its high symmetry. With this strategy, we enabled two different ferritin nanocages to disassemble into protein tetramers under neutral solution by introducing His6 motifs at the 4-fold channel interfaces. Notably, these tetramers are able to self-assemble into ferritin-like protein nanocages in response to multiple external stimuli such as transition metal ions and pH, and vice versa, indicative of a reversible self-assembly process. Furthermore, such His-mediated reversible protein self-assembly has been explored for encapsulation of bioactive cargo molecules within these reconstituted protein nanocages with higher loading efficiency under milder conditions as compared to the reported acid denaturation encapsulation method for ferritin. | |||
His-Mediated Reversible Self-Assembly of Ferritin Nanocages through Two Different Switches for Encapsulation of Cargo Molecules.,Gu C, Zhang T, Lv C, Liu Y, Wang Y, Zhao G ACS Nano. 2020 Nov 16. doi: 10.1021/acsnano.0c06670. PMID:33197176<ref>PMID:33197176</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7cpc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ferritin 3D structures|Ferritin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Penaeus japonicus]] | |||
[[Category: Gu C]] | |||
[[Category: Zhang T]] | |||
[[Category: Zhao G]] | |||
Latest revision as of 19:13, 29 November 2023
His-Mediated Reversible Self-assembly of Ferritin Nanocage with Ni bindingHis-Mediated Reversible Self-assembly of Ferritin Nanocage with Ni binding
Structural highlights
FunctionT2B7E1_PENJP 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] Publication Abstract from PubMedProtein nanocages represent a class of nanovehicles for a variety of applications. However, precise manipulation of self-assembly behavior of these protein nanocages in response to multiple external stimuli for custom-tailored applications remains challenging. Herein, we established a simple but effective strategy for controlling protein nanocage self-assembly that combines a dual property of His motifs (their significantly pH-dependent protonation state and their capacity to coordinate with transition metals) with its high symmetry. With this strategy, we enabled two different ferritin nanocages to disassemble into protein tetramers under neutral solution by introducing His6 motifs at the 4-fold channel interfaces. Notably, these tetramers are able to self-assemble into ferritin-like protein nanocages in response to multiple external stimuli such as transition metal ions and pH, and vice versa, indicative of a reversible self-assembly process. Furthermore, such His-mediated reversible protein self-assembly has been explored for encapsulation of bioactive cargo molecules within these reconstituted protein nanocages with higher loading efficiency under milder conditions as compared to the reported acid denaturation encapsulation method for ferritin. His-Mediated Reversible Self-Assembly of Ferritin Nanocages through Two Different Switches for Encapsulation of Cargo Molecules.,Gu C, Zhang T, Lv C, Liu Y, Wang Y, Zhao G ACS Nano. 2020 Nov 16. doi: 10.1021/acsnano.0c06670. PMID:33197176[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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