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Encapsulin - Wikipedia

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EM structure of Myxococcus xanthus encpasulin protein (EncA) PDB entry 4pt2

Identifiers

Symbol

Linocin_M18

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

The encapsulins are a family of bacterial proteins that serve as the main structural components of encapsulin nanocompartments.^[1] There are several different encapsulin proteins, including EncA, which forms the shell, and EncB, EncC, and EncD, which form the core.^[1]

Encapsulins are also used in synthetic biology. They are hard to discover due to their similarity to phage proteins.^[2]

History

Encapsulins were discovered in 1994 as a new class of prokaryotic compartments.^[3] Prokaryotic cells usually lack membrane compartments typical for eukaryotes. They instead have numerous protein compartments that are capable of accumulating a large number of molecules.^[3]

When protein nanocompartments were discovered in 1994, and later renamed encapsulins, they were found in the supernatant fluid of the Brevibacterium linens culture.^[3]

In 2008, encapsulins were recognized as protein-based compartmentalization systems with dedicated functions in cellular organisms.^[4]

Structure

Encapsulin shells compromise icosahedral complexes (12 vertices, 20 faces, 30 edges) formed as a result of self-assembly of protomers. ^[3] The shells have diameters between 24 and 42 nm and are defined by the viral HK97-fold of their shell protein. ^[4] The HK97-fold protomer is roughly triangular and has three conserved domains, the axial domain, peripheral domain, and extended loop.^[4]

Function

Encapsulins serve many physiological functions, including catalysis, mineral storage, response to oxidative stress and secondary metabolism. There are ferritin-like encapsulins as well.^[2]

References

^ ^a ^b McHugh CA, Fontana J, Nemecek D, Cheng N, Aksyuk AA, Heymann JB, Winkler DC, Lam AS, Wall JS, Steven AC, Hoiczyk E (September 2014). "A virus capsid-like nanocompartment that stores iron and protects bacteria from oxidative stress". The EMBO Journal. 33 (17): 1896–911. doi:10.15252/embj.201488566. PMC 4195785. PMID 25024436.
^ ^a ^b Kashif-Khan N, Savva R, Frank S (7 March 2024). "Mining metagenomics data for novel bacterial nanocompartments". NAR Genomics & Bioinformatics. 6 (1): lqae025. doi:10.1093/nargab/lqae025.
^ ^a ^b ^c ^d Chmelyuk, Nelly S.; Oda, Vera V.; Gabashvili, Anna N.; Abakumov, Maxim A. (17 Feb 2023). "Encapsulins: Structure, Properties, and Biotechnological Applications". Biochemistry (Moscow). 88 (1): 35–49. doi:10.1134/S0006297923010042. ISSN 0006-2979. PMC 9937530. Retrieved 17 Oct 2024 – via National Library of Medicine.
^ ^a ^b ^c Giessen, Tobias W. (18 Mar 2022). "Encapsulins". Annual Review of Biochemistry. 91 (1): 353–380. doi:10.1146/annurev-biochem-040320-102858. ISSN 0066-4154. PMC 9944552. PMID 35303791.

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