9s05

Focused refinement of open encapsulin pentamer from symmetry expansion of icosahedral single particle reconstruction of the Rhodospirillum rubrum encapsulin:encapsulated ferritin complex

spinqualitylabelsall models 9s05, resolution 2.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9s05 is a 10 chain structure with sequence from Rhodospirillum rubrum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.68Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FER_RHORT Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like ferroxidase that mineralizes iron inside the encapsulin nanocompartment. Converts Fe(2+) to Fe(3+) that is released to the exterior of the decameric complex for deposition in the encapsulin nanocompartment. In solution the decamer binds 10-15 iron cations; in the encapsulin nanocompartment the decamer can bind up to 48 ions, perhaps via its internal channel and on its exterior. The empty encapsulin nanocompartment sequesters about 2200 Fe ions while the cargo-loaded nanocompartment can maximally sequester about 4150 Fe ions. EncFtn retains ferroxidase activity when encapsulated (PubMed:27529188). Flux in the active site di-iron metal center is thought to be controlled by the 'entry site' of the protein, which both attracts metal and controls the rate of iron oxidation (Probable). Encapsulation in the nanocompartment does not alter either function of this protein (PubMed:32878987).

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