9fn9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Icosahedral Encapsulin with a closed pore state== | |
| + | <StructureSection load='9fn9' size='340' side='right'caption='[[9fn9]], [[Resolution|resolution]] 2.81Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9fn9]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FN9 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]] 2.81Å</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=9fn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fn9 OCA], [https://pdbe.org/9fn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fn9 RCSB], [https://www.ebi.ac.uk/pdbsum/9fn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fn9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0R4H0_MYCS2 A0R4H0_MYCS2] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nitroreductases are important enzymes for a variety of applications, including cancer therapy and bioremediation. They often require encapsulation to improve stability and activity. We focus on genetically encoded encapsulation of nitroreductases within protein capsids, like encapsulins. Our study showcases the encapsulation of nitroreductase NfsB as functional dimers within encapsulins, which enhances protein activity and stability in diverse conditions. Mutations within the pore region are beneficial for activity of the encapsulated enzyme, potentially by increasing diffusion rates. Cryogenic electron microscopy reveals the overall architecture of the encapsulated dimeric NfsB within the nanoreactor environment and identifies multiple pore states in the shell. These findings highlight the potential of encapsulins as versatile tools for enhancing enzyme performance across various fields. | ||
| - | + | A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor.,Zmyslia M, Capper MJ, Grimmeisen M, Sartory K, Deuringer B, Abdelsalam M, Shen K, Jung M, Sippl W, Koch HG, Kaul L, Suss R, Kohnke J, Jessen-Trefzer C RSC Chem Biol. 2024 Nov 4;6(1):21-35. doi: 10.1039/d4cb00127c. PMID:39508026<ref>PMID:39508026</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9fn9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycolicibacterium smegmatis MC2 155]] | ||
| + | [[Category: Capper MJ]] | ||
| + | [[Category: Kohhnke J]] | ||
Current revision
Icosahedral Encapsulin with a closed pore state
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