| Structural highlights
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).[1] [2] [3]
References
- ↑ He D, Hughes S, Vanden-Hehir S, Georgiev A, Altenbach K, Tarrant E, Mackay CL, Waldron KJ, Clarke DJ, Marles-Wright J. Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments. Elife. 2016 Aug 16;5. pii: e18972. doi: 10.7554/eLife.18972. PMID:27529188 doi:http://dx.doi.org/10.7554/eLife.18972
- ↑ Piergentili C, Ross J, He D, Gallagher KJ, Stanley WA, Adam L, Mackay CL, Basle A, Waldron KJ, Clarke DJ, Marles-Wright J. Dissecting the structural and functional roles of a putative metal entry site in encapsulated ferritins. J Biol Chem. 2020 Sep 2. pii: RA120.014502. doi: 10.1074/jbc.RA120.014502. PMID:32878987 doi:http://dx.doi.org/10.1074/jbc.RA120.014502
- ↑ Piergentili C, Ross J, He D, Gallagher KJ, Stanley WA, Adam L, Mackay CL, Basle A, Waldron KJ, Clarke DJ, Marles-Wright J. Dissecting the structural and functional roles of a putative metal entry site in encapsulated ferritins. J Biol Chem. 2020 Sep 2. pii: RA120.014502. doi: 10.1074/jbc.RA120.014502. PMID:32878987 doi:http://dx.doi.org/10.1074/jbc.RA120.014502
|