7xa2

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'''Unreleased structure'''
 
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The entry 7xa2 is ON HOLD until Paper Publication
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==Thermotoga maritima ferritin variant-Tm-E(S111H)==
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<StructureSection load='7xa2' size='340' side='right'caption='[[7xa2]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7xa2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XA2 FirstGlance]. <br>
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</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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xa2 OCA], [https://pdbe.org/7xa2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xa2 RCSB], [https://www.ebi.ac.uk/pdbsum/7xa2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xa2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9X0L2_THEMA Q9X0L2_THEMA] Iron storage protein (By similarity).[RuleBase:RU361145]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Engineering proteins to construct self-assemblies is of crucial significance not only for understanding the sophisticated living systems but also for fabricating advanced materials with unexplored functions. However, due to the inherent chemical heterogeneity and structural complexity of the protein surface, designing complex protein assemblies in an anisotropic fashion remains challenging. Here, we describe a self-assembly approach to fabricating protein origami with a networklike structure by designing dual noncovalent interactions on the different positions of a single protein building block. With dimeric proteins as building blocks, 1D protein filaments were constructed by the designed metal coordination at key protein interfaces. Subsequently, the network superstructures were created by the cross-linking of the 1D protein filaments at branch point linkages through the second designed pi-pi stacking interactions. Notably, upon increasing the protein concentration, the formed protein networks convert into hydrogels with reversible, injectable, and self-healing properties, which have the ability to promote bone regeneration. This strategy could be used to fabricate other protein-based materials with unexplored functions.
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Authors: Yu, L., Guanghua, Z.
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Directed Self-Assembly of Dimeric Building Blocks into Networklike Protein Origami to Construct Hydrogels.,Liu Y, Chen X, Yin S, Chang X, Lv C, Zang J, Leng X, Zhang T, Zhao G ACS Nano. 2022 Nov 22;16(11):19472-19481. doi: 10.1021/acsnano.2c09391. Epub 2022 , Oct 31. PMID:36315654<ref>PMID:36315654</ref>
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Description: Thermotoga maritima ferritin variant-Tm-E(S111H)
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Guanghua, Z]]
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<div class="pdbe-citations 7xa2" style="background-color:#fffaf0;"></div>
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[[Category: Yu, L]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermotoga maritima]]
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[[Category: Liu Y]]
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[[Category: Zhao G]]

Revision as of 10:24, 15 February 2023

Thermotoga maritima ferritin variant-Tm-E(S111H)

PDB ID 7xa2

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