7ODW

Model of Haliangium ochraceum encapsulin from icosahedral single particle reconstruction

Summary for 7ODW

• Entry DOI: 10.2210/pdb7odw/pdb
• EMDB information: 12853
• Descriptor: Linocin_M18 bacteriocin protein (1 entity in total)
• Functional Keywords: encapsulin, encapsulated ferritin, haliangium ochraceum, virus like particle
• Biological source: Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2)
• Total number of polymer chains: 1
• Total formula weight: 28844.60

Authors

Marles-Wright, J.,Basle, A.,Clarke, D.J.,Ross, J. (deposition date: 2021-04-30, release date: 2022-03-09, Last modification date: 2024-07-10)

Primary citation

Ross, J.,McIver, Z.,Lambert, T.,Piergentili, C.,Bird, J.E.,Gallagher, K.J.,Cruickshank, F.L.,James, P.,Zarazua-Arvizu, E.,Horsfall, L.E.,Waldron, K.J.,Wilson, M.D.,Mackay, C.L.,Basle, A.,Clarke, D.J.,Marles-Wright, J.
Pore dynamics and asymmetric cargo loading in an encapsulin nanocompartment.
Sci Adv, 8:eabj4461-eabj4461, 2022

PubMed Abstract: Encapsulins are protein nanocompartments that house various cargo enzymes, including a family of decameric ferritin-like proteins. Here, we study a recombinant 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.

PubMed: 35080974
DOI: 10.1126/sciadv.abj4461

Experimental method

ELECTRON MICROSCOPY (2.5 Å)