EMD-13603

Single-particle
3.24 Å
EMD-13603 Deposition: 20/09/2021
Map released: 09/02/2022
Last modified: 09/02/2022
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-13603

Asymmetric single particle reconstruction of the Haliangium ochraceum encapsulin encapsulated ferritin complex calculated using Cryosparc

EMD-13603

Single-particle
3.24 Å
EMD-13603 Deposition: 20/09/2021
Map released: 09/02/2022
Last modified: 09/02/2022
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Haliangium ochraceum
Sample: Ternary complex of Haliangium ochraceum encapsulin and encapsulated ferritin proteins

Deposition Authors: Marles-Wright J , Basle A , Ross J , Clarke DJ
Pore dynamics and asymmetric cargo loading in an encapsulin nanocompartment.
PUBMED: 35080974
DOI: doi:10.1126/sciadv.abj4461
ISSN: 2375-2548
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.