Journal
ELIFE
Volume 5, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.18972
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Funding
- China Scholarship Council
- University Of Edinburgh
- Wellcome Trust [098375/Z/12/Z]
- Biotechnology and Biological Sciences Research Council [BB/N005570/1]
- Royal Society [RG130585]
- Wellcome Trust [098375/Z/12/Z] Funding Source: Wellcome Trust
- BBSRC [BB/N005570/1] Funding Source: UKRI
- EPSRC [EP/K039717/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/N005570/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/K039717/1] Funding Source: researchfish
- Wellcome Trust [098375/Z/12/Z] Funding Source: researchfish
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Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage. We have characterized the structure and function of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid. We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface. EncFtn adopts an open decameric structure that is topologically distinct from other ferritins. While EncFtn acts as a ferroxidase, it cannot mineralize iron. Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage. This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.
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