Difference between revisions of "Part:BBa K4229020"

Revision as of 17:13, 11 October 2022

Encapsulin

Encapsulins are nanocompartments, which similar to microcompartments, are self-assembled- protein-compartments natively found in some bacteria and Archaea [1] . They can be distinguished from microcompartments based on the size of the compartments (20-32 nm) [1]. Their icosahedral shape resembles the HK97 bacteriophage capsid [2]. Multiple encapsulins encapsulate cargo protein based on a short C-terminal peptide sequence, called the target peptide

[1] T. W. Giessen, “Encapsulins: Microbial nanocompartments with applications in biomedicine, nanobiotechnology and materials science,” Curr. Opin. Chem. Biol., vol. 34, pp. 1–10, 2016, doi: 10.1016/j.cbpa.2016.05.013.

[2]J. Fontana et al., “Phage capsid-like structure of Myxococcus xanthus encapsulin, a protein shell that stores iron,” Microsc. Microanal., vol. 20, no. 3, pp. 1244–1245, 2014, doi: 10.1017/S1431927614007958. Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 [1] T. W. Giessen, “Encapsulins: Microbial nanocompartments with applications in biomedicine, nanobiotechnology and materials science,” Curr. Opin. Chem. Biol., vol. 34, pp. 1–10, 2016, doi: 10.1016/j.cbpa.2016.05.013.
 [2]J. Fontana et al., “Phage capsid-like structure of Myxococcus xanthus encapsulin, a protein shell that stores iron,” Microsc. Microanal., vol. 20, no. 3, pp. 1244–1245, 2014, doi: 10.1017/S1431927614007958.
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