PMID- 27529188 OWN - NLM STAT- MEDLINE DCOM- 20171030 LR - 20210620 IS - 2050-084X (Electronic) IS - 2050-084X (Linking) VI - 5 DP - 2016 Aug 16 TI - Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments. LID - e18972 [pii] LID - 10.7554/eLife.18972 [doi] AB - 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. FAU - He, Didi AU - He D AUID- ORCID: 0000-0002-3360-9352 AD - Institute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, United Kingdom. FAU - Hughes, Sam AU - Hughes S AD - The School of Chemistry, The University of Edinburgh, Edinburgh, United Kingdom. FAU - Vanden-Hehir, Sally AU - Vanden-Hehir S AD - The School of Chemistry, The University of Edinburgh, Edinburgh, United Kingdom. FAU - Georgiev, Atanas AU - Georgiev A AD - Institute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, United Kingdom. FAU - Altenbach, Kirsten AU - Altenbach K AD - Institute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, United Kingdom. FAU - Tarrant, Emma AU - Tarrant E AD - Institute for Cell and Molecular Biosciences, Newcastle University, Newcasle upon Tyne, United Kingdom. FAU - Mackay, C Logan AU - Mackay CL AD - The School of Chemistry, The University of Edinburgh, Edinburgh, United Kingdom. FAU - Waldron, Kevin J AU - Waldron KJ AUID- ORCID: 0000-0002-5577-7357 AD - Institute for Cell and Molecular Biosciences, Newcastle University, Newcasle upon Tyne, United Kingdom. FAU - Clarke, David J AU - Clarke DJ AUID- ORCID: 0000-0002-3741-2952 AD - The School of Chemistry, The University of Edinburgh, Edinburgh, United Kingdom. FAU - Marles-Wright, Jon AU - Marles-Wright J AUID- ORCID: 0000-0002-9156-3284 AD - Institute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, United Kingdom. AD - School of Biology, Newcastle University, Newcastle upon Tyne, United Kingdom. LA - eng GR - WT_/Wellcome Trust/United Kingdom GR - 098375/Z/12/Z/WT_/Wellcome Trust/United Kingdom GR - BB/N005570/1/BB_/Biotechnology and Biological Sciences Research Council/United Kingdom PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20160816 PL - England TA - Elife JT - eLife JID - 101579614 RN - 9007-73-2 (Ferritins) RN - E1UOL152H7 (Iron) RN - EC 1.16.3.1 (Ceruloplasmin) SB - IM MH - Ceruloplasmin/chemistry/metabolism MH - Crystallography, X-Ray MH - Ferritins/*chemistry/*metabolism MH - Iron/*metabolism MH - Microscopy, Electron, Transmission MH - Models, Molecular MH - Protein Conformation MH - Protein Multimerization MH - Rhodospirillum rubrum/*enzymology/*metabolism PMC - PMC5012862 OTO - NOTNLM OT - Rhodospirillum rubrum OT - biochemistry OT - biophysics OT - encapsulated ferritin OT - encapsulin OT - ferritin OT - structural biology COIS- The authors declare that no competing interests exist. EDAT- 2016/08/17 06:00 MHDA- 2017/10/31 06:00 PMCR- 2016/08/17 CRDT- 2016/08/17 06:00 PHST- 2016/06/24 00:00 [received] PHST- 2016/08/14 00:00 [accepted] PHST- 2016/08/17 06:00 [entrez] PHST- 2016/08/17 06:00 [pubmed] PHST- 2017/10/31 06:00 [medline] PHST- 2016/08/17 00:00 [pmc-release] AID - e18972 [pii] AID - 18972 [pii] AID - 10.7554/eLife.18972 [doi] PST - epublish SO - Elife. 2016 Aug 16;5:e18972. doi: 10.7554/eLife.18972.