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Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments

Lookup NU author(s): Dr Emma Tarrant, Dr Kevin WaldronORCiD, Dr Jon Marles-WrightORCiD



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


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.

Publication metadata

Author(s): He D, Hughes S, Vanden-Hehir S, Georgiev A, Altenbach K, Tarrant E, Mackay CL, Waldron KJ, Clarke DJ, Marles-Wright J

Publication type: Article

Publication status: Published

Journal: eLife

Year: 2016

Volume: 5

Online publication date: 16/08/2016

Acceptance date: 14/08/2016

Date deposited: 20/09/2016

ISSN (electronic): 2050-084X

Publisher: eLife Sciences Publications Ltd


DOI: 10.7554/eLife.18972


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Funder referenceFunder name
China Scholarship Council
University Of Edinburgh
098375/Z/12/ZWellcome Trust
BB/N005570/1Biotechnology and Biological Sciences Research Council
RG130585Royal Society