9B9Q
Cargo-loaded Myxococcus xanthus EncA encapsulin engineered pore mutant with T=3 icosahedral symmetry
Summary for 9B9Q
| Entry DOI | 10.2210/pdb9b9q/pdb |
| EMDB information | 44388 |
| Descriptor | Type 1 encapsulin shell protein EncA, Encapsulin nanocompartment cargo protein EncC (2 entities in total) |
| Functional Keywords | encapsulin, nanocompartment, pore mutant, virus like particle |
| Biological source | Myxococcus xanthus DK 1622 More |
| Total number of polymer chains | 6 |
| Total formula weight | 96950.10 |
| Authors | Andreas, M.P.,Kwon, S.,Giessen, T.W. (deposition date: 2024-04-03, release date: 2024-09-18, Last modification date: 2024-09-25) |
| Primary citation | Kwon, S.,Andreas, M.P.,Giessen, T.W. Pore Engineering as a General Strategy to Improve Protein-Based Enzyme Nanoreactor Performance. Acs Nano, 18:25740-25753, 2024 Cited by PubMed Abstract: Enzyme nanoreactors are nanoscale compartments consisting of encapsulated enzymes and a selectively permeable barrier. Sequestration and colocalization of enzymes can increase catalytic activity, stability, and longevity, highly desirable features for many biotechnological and biomedical applications of enzyme catalysts. One promising strategy to construct enzyme nanoreactors is to repurpose protein nanocages found in nature. However, protein-based enzyme nanoreactors often exhibit decreased catalytic activity, partially caused by a mismatch of protein shell selectivity and the substrate requirements of encapsulated enzymes. No broadly applicable and modular protein-based nanoreactor platform is currently available. Here, we introduce a pore-engineered universal enzyme nanoreactor platform based on encapsulins-microbial self-assembling protein nanocompartments with programmable and selective enzyme packaging capabilities. We structurally characterize our protein shell designs via cryo-electron microscopy and highlight their polymorphic nature. Through fluorescence polarization assays, we show their improved molecular flux behavior and highlight their expanded substrate range via a number of proof-of-concept enzyme nanoreactor designs. This work lays the foundation for utilizing our encapsulin-based nanoreactor platform for diverse future biotechnological and biomedical applications. PubMed: 39226211DOI: 10.1021/acsnano.4c08186 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.14 Å) |
Structure validation
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