Pore dynamics and asymmetric cargo loading in an encapsulin nanocompartment

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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 languageEnglish
Article numbereabj4461
JournalScience Advances
Issue number4
Early online date26 Jan 2022
Publication statusE-pub ahead of print - 26 Jan 2022


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