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| Title | A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor. |
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| Journal, issue, pages | RSC Chem Biol, Vol. 6, Issue 1, Page 21-35, Year 2024 |
| Publish date | Nov 4, 2024 |
Authors | Mariia Zmyslia / Michael J Capper / Michael Grimmeisen / Kerstin Sartory / Benedikt Deuringer / Mohamed Abdelsalam / Kaiwei Shen / Manfred Jung / Wolfgang Sippl / Hans-Georg Koch / Laurine Kaul / Regine Süss / Jesko Köhnke / Claudia Jessen-Trefzer / ![]() |
| PubMed Abstract | 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 ...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. |
External links | RSC Chem Biol / PubMed:39508026 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.22 - 2.81 Å |
| Structure data | EMDB-50585, PDB-9fn9: EMDB-50586, PDB-9fna: |
| Source |
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Keywords | BIOSYNTHETIC PROTEIN / Nanocompartment |
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