5DA5

Crystal structure of Rhodospirillum rubrum Rru_A0973

Summary for 5DA5

• Entry DOI: 10.2210/pdb5da5/pdb
• Descriptor: Rru_A0973, FE (III) ION, GLYCOLIC ACID, ... (5 entities in total)
• Functional Keywords: ferritin, iron, ferroxidase, oxidoreductase
• Biological source: Rhodospirillum rubrum
• Total number of polymer chains: 30
• Total formula weight: 404444.60

Authors

He, D.,Vanden Hehier, S.,Georgiev, A.,Altenbach, K.,Tarrant, E.,Mackay, C.L.,Waldron, K.J.,Clarke, D.J.,Marles-Wright, J. (deposition date: 2015-08-19, release date: 2016-08-10, Last modification date: 2024-01-10)

Primary citation

He, D.,Hughes, S.,Vanden-Hehir, S.,Georgiev, A.,Altenbach, K.,Tarrant, E.J.,Mackay, C.L.,Waldron, K.J.,Clarke, D.J.,Marles-Wright, J.
Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments.
Elife, 5:-, 2016

PubMed 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.

PubMed: 27529188
DOI: 10.7554/eLife.18972

Experimental method

X-RAY DIFFRACTION (2.064 Å)