Pore dynamics and asymmetric cargo loading in an encapsulin nanocompartment

Autor: Jennifer Ross, Zak McIver, Thomas Lambert, Cecilia Piergentili, Jasmine Emma Bird, Kelly J. Gallagher, Faye L. Cruickshank, Patrick James, Efrain Zarazúa-Arvizu, Louise E. Horsfall, Kevin J. Waldron, Marcus D. Wilson, C. Logan Mackay, Arnaud Baslé, David J. Clarke, Jon Marles-Wright
Rok vydání: 2022
Předmět:
Zdroj: Ross, J, McIver, Z, Lambert, T, Piergentili, C, Bird, J E, Gallagher, K J, Cruickshank, F L, James, P, Zarazúa-Arvizu, E, Horsfall, L E, Waldron, K J, Wilson, M D, Logan Mackay, C, Baslé, A, Clarke, D J & Marles-Wright, J 2022, ' Pore dynamics and asymmetric cargo loading in an encapsulin nanocompartment ', Science Advances, vol. 8, no. 4, eabj4461 . https://doi.org/10.1126/sciadv.abj4461
ISSN: 2375-2548
DOI: 10.1126/sciadv.abj4461
Popis: 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.
Databáze: OpenAIRE
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