9BHV
Streptomyces griseus Family 2B encapsulin shell with 2-methylisoborneol synthase cargo
Summary for 9BHV
| Entry DOI | 10.2210/pdb9bhv/pdb |
| EMDB information | 44554 |
| Descriptor | Nucleotide-binding protein, CALCIUM ION (2 entities in total) |
| Functional Keywords | encapsulin, nanocompartment, virus like particle |
| Biological source | Streptomyces griseus subsp. griseus |
| Total number of polymer chains | 1 |
| Total formula weight | 52054.22 |
| Authors | |
| Primary citation | Andreas, M.P.,Giessen, T.W. The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell. Nat Commun, 15:9715-9715, 2024 Cited by PubMed Abstract: Terpenoids are the largest class of natural products, found across all domains of life. One of the most abundant bacterial terpenoids is the volatile odorant 2-methylisoborneol (2-MIB), partially responsible for the earthy smell of soil and musty taste of contaminated water. Many bacterial 2-MIB biosynthetic gene clusters were thought to encode a conserved transcription factor, named EshA in the model soil bacterium Streptomyces griseus. Here, we revise the function of EshA, now referred to as Sg Enc, and show that it is a Family 2B encapsulin shell protein. Using cryo-electron microscopy, we find that Sg Enc forms an icosahedral protein shell and encapsulates 2-methylisoborneol synthase (2-MIBS) as a cargo protein. Sg Enc contains a cyclic adenosine monophosphate (cAMP) binding domain (CBD)-fold insertion and a unique metal-binding domain, both displayed on the shell exterior. We show that Sg Enc CBDs do not bind cAMP. We find that 2-MIBS cargo loading is mediated by an N-terminal disordered cargo-loading domain and that 2-MIBS activity and Sg Enc shell structure are not modulated by cAMP. Our work redefines the function of EshA and establishes Family 2B encapsulins as cargo-loaded protein nanocompartments involved in secondary metabolite biosynthesis. PubMed: 39521781DOI: 10.1038/s41467-024-54175-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.02 Å) |
Structure validation
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