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

Didi He, Sam Hughes, Sally Vanden-hehir, Atanas Georgiev, Kirsten Altenbach, Emma Tarrant, C Logan Mackay, Kevin J Waldron, David J Clarke, Jon Marles-wright

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Article numbere18972
JournaleLIFE
Volume5
Early online date16 Aug 2016
DOIs
Publication statusPublished - 16 Aug 2016

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