9FNA の概要
| エントリーDOI | 10.2210/pdb9fna/pdb |
| EMDBエントリー | 50586 |
| 分子名称 | 29 kDa antigen Cfp29 (1 entity in total) |
| 機能のキーワード | nanocompartment, biosynthetic protein |
| 由来する生物種 | Mycolicibacterium smegmatis |
| タンパク質・核酸の鎖数 | 60 |
| 化学式量合計 | 1802734.68 |
| 構造登録者 | |
| 主引用文献 | Zmyslia, M.,Capper, M.J.,Grimmeisen, M.,Sartory, K.,Deuringer, B.,Abdelsalam, M.,Shen, K.,Jung, M.,Sippl, W.,Koch, H.G.,Kaul, L.,Suss, R.,Kohnke, J.,Jessen-Trefzer, C. A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor. Rsc Chem Biol, 6:21-35, 2024 Cited by 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 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. PubMed: 39508026DOI: 10.1039/d4cb00127c 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.22 Å) |
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