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Abstract
Encapsulins are protein nanocompartments that house various cargo enzymes, including a family of decameric ferritin-like proteins. Here, we study a recombinant Haliangium ochraceum encapsulin:encapsulated ferritin complex using cryo–electron microscopy and hydrogen/deuterium exchange mass spectrometry to gain insight into the structural relationship between the encapsulin shell and its protein cargo. An asymmetric single-particle reconstruction reveals four encapsulated ferritin decamers in a tetrahedral arrangement within the encapsulin nanocompartment. This leads to a symmetry mismatch between the protein cargo and the icosahedral encapsulin shell. The encapsulated ferritin decamers are offset from the interior face of the encapsulin shell. Using hydrogen/ deuterium exchange mass spectrometry, we observed the dynamic behavior of the major fivefold pore in the encapsulin shell and show the pore opening via the movement of the encapsulin A-domain. These data will accelerate efforts to engineer the encapsulation of heterologous cargo proteins and to alter the permeability of the encapsulin shell via pore modifications.
Original language | English |
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Article number | eabj4461 |
Journal | Science Advances |
Volume | 8 |
Issue number | 4 |
Early online date | 26 Jan 2022 |
DOIs | |
Publication status | E-pub ahead of print - 26 Jan 2022 |
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Recruitment of BRCA1-A complex to nucleosomes and sites of DNA damage
1/09/20 → 31/08/23
Project: Research
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Mechanistic understanding of the reading and writing of DNA methylation¿¿¿
1/07/18 → 1/11/23
Project: Research