7oeu

Model of open pentamer of the Haliangium ochraceum encapsulin from symmetry expansion of icosahedral single particle reconstruction

spinqualitylabelsall models 7oeu, resolution 2.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7oeu is a 10 chain structure with sequence from Haliangium ochraceum DSM 14365. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.64Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ENCAP_HALO1 Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells about 21 nm in diameter. Small pores form at, or close to, the 2-, 3-, and 5-fold symmetry axes. Data analysis suggests the 5-fold pores open and close with maximal and minimal aperatures of 15 and 5 Angstroms. Cargo protein Fer (ferritin-like protein, probably stores iron) is targeted to the interior via its C-terminal extension; empty intact shells can be isolated in the absence of cargo protein. Publication Abstract from PubMed 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. Pore dynamics and asymmetric cargo loading in an encapsulin nanocompartment.,Ross J, McIver Z, Lambert T, Piergentili C, Bird JE, Gallagher KJ, Cruickshank FL, James P, Zarazua-Arvizu E, Horsfall LE, Waldron KJ, Wilson MD, Mackay CL, Basle A, Clarke DJ, Marles-Wright J Sci Adv. 2022 Jan 28;8(4):eabj4461. doi: 10.1126/sciadv.abj4461. Epub 2022 Jan, 26. PMID:35080974 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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