9FNA

CryoEM structure of Encapsulin::tdNfsB with an open pore state

This is a non-PDB format compatible entry.

Summary for 9FNA

• Entry DOI: 10.2210/pdb9fna/pdb
• EMDB information: 50586
• Descriptor: 29 kDa antigen Cfp29 (1 entity in total)
• Functional Keywords: nanocompartment, biosynthetic protein
• Biological source: Mycolicibacterium smegmatis
• Total number of polymer chains: 60
• Total formula weight: 1802734.68

Authors

Capper, M.J.,Kohhnke, J. (deposition date: 2024-06-09, release date: 2025-03-19)

Primary citation

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

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: 39508026
DOI: 10.1039/d4cb00127c

Experimental method

ELECTRON MICROSCOPY (2.22 Å)