9fn9 | pdb_00009fn9

Icosahedral Encapsulin with a closed pore state

spinqualitylabelsall models 9fn9, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9fn9 is a 60 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.81Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0R4H0_MYCS2 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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