Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments
- The University of Edinburgh, United Kingdom
- Newcastle University, United Kingdom
- Cited 16
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Abstract
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.
Article and author information
Author details
Funding
Royal Society (RG130585)
- Jon Marles-Wright
China Scholarship Council
- Didi He
Biotechnology and Biological Sciences Research Council (BB/N005570/1)
- David J Clarke
- Jon Marles-Wright
Wellcome Trust (098375/Z/12/Z)
- Emma J Tarrant
- Kevin J Waldron
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Reviewing Editor
- Richard Losick, Harvard University, United States
Publication history
- Received: June 24, 2016
- Accepted: August 14, 2016
- Accepted Manuscript published: August 16, 2016 (version 1)
- Accepted Manuscript updated: August 24, 2016 (version 2)
- Version of Record published: September 6, 2016 (version 3)
Copyright
© 2016, He et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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