6I9G
Crystal structure of encapsulin from Mycolicibacterium hassiacum
Summary for 6I9G
| Entry DOI | 10.2210/pdb6i9g/pdb |
| Descriptor | Linocin-M18, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | nanocompartment, nanocage, packaging of biocatalysts, bacteriocin, virus like particle |
| Biological source | Mycolicibacterium hassiacum DSM 44199 |
| Total number of polymer chains | 15 |
| Total formula weight | 446809.81 |
| Authors | Rozeboom, H.J.,Fraaije, M.W. (deposition date: 2018-11-23, release date: 2019-12-04, Last modification date: 2024-11-06) |
| Primary citation | Loncar, N.,Rozeboom, H.J.,Franken, L.E.,Stuart, M.C.A.,Fraaije, M.W. Structure of a robust bacterial protein cage and its application as a versatile biocatalytic platform through enzyme encapsulation. Biochem.Biophys.Res.Commun., 529:548-553, 2020 Cited by PubMed Abstract: Using a newly discovered encapsulin from Mycolicibacterium hassiacum, several biocatalysts were packaged in this robust protein cage. The encapsulin was found to be easy to produce as recombinant protein. Elucidation of its crystal structure revealed that it is a spherical protein cage of 60 protomers (diameter of 23 nm) with narrow pores. By developing an effective coexpression and isolation procedure, the effect of packaging a variety of biocatalysts could be evaluated. It was shown that encapsulation results in a significantly higher stability of the biocatalysts. Most of the targeted cofactor-containing biocatalysts remained active in the encapsulin. Due to the restricted diameters of the encapsulin pores (5-9 Å), the protein cage protects the encapsulated enzymes from bulky compounds. The work shows that encapsulins may be valuable tools to tune the properties of biocatalysts such as stability and substrate specificity. PubMed: 32736672DOI: 10.1016/j.bbrc.2020.06.059 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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