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TitlePore dynamics and asymmetric cargo loading in an encapsulin nanocompartment.
Journal, issue, pagesSci Adv, Vol. 8, Issue 4, Page eabj4461, Year 2022
Publish dateJan 28, 2022
AuthorsJennifer 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 /
PubMed AbstractEncapsulins are protein nanocompartments that house various cargo enzymes, including a family of decameric ferritin-like proteins. Here, we study a recombinant encapsulin:encapsulated ferritin ...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.
External linksSci Adv / PubMed:35080974 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 5.5 Å
Structure data

12853

7odw

EMDB-12853: Icosahedral cryo-EM reconstruction of Haliangium ochraceum encapsulin
PDB-7odw: Model of Haliangium ochraceum encapsulin from icosahedral single particle reconstruction
Method: EM (single particle) / Resolution: 2.5 Å

12859

7oe2

EMDB-12859, PDB-7oe2:
Model of closed pentamer of the Haliangium ochraceum encapsulin from symmetry expansion of icosahedral single particle reconstruction
Method: EM (single particle) / Resolution: 2.4 Å

12864

7oeu

EMDB-12864: Single particle reconstruction of open pentamer of the Haliangium ochraceum encapsulin from symmetry expansion of icosahedral single particle reconstruction
PDB-7oeu: Model of open pentamer of the Haliangium ochraceum encapsulin from symmetry expansion of icosahedral single particle reconstruction
Method: EM (single particle) / Resolution: 2.64 Å

EMDB-12873:
Asymmetric single particle reconstruction of the Haliangium ochraceum encapsulin encapsulated ferritin complex
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-13603:
Asymmetric single particle reconstruction of the Haliangium ochraceum encapsulin encapsulated ferritin complex calculated using Cryosparc
Method: EM (single particle) / Resolution: 3.24 Å

EMDB-13608: Focused reconstruction of Haliangium ochraceum encapsulated ferritin cargo within the encapsulin nano compartment
Method: EM (single particle) / Resolution: 5.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • Haliangium ochraceum (bacteria)
  • haliangium ochraceum (strain dsm 14365 / jcm 11303 / smp-2) (bacteria)
KeywordsVIRUS LIKE PARTICLE / Encapsulin / encapsulated ferritin / haliangium ochraceum

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