PMID- 30837306
OWN - NLM
STAT- MEDLINE
DCOM- 20191218
LR  - 20191218
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 476
IP  - 6
DP  - 2019 Mar 22
TI  - Conservation of the structural and functional architecture of encapsulated 
      ferritins in bacteria and archaea.
PG  - 975-989
LID - 10.1042/BCJ20180922 [doi]
AB  - Ferritins are a large family of intracellular proteins that protect the cell from 
      oxidative stress by catalytically converting Fe(II) into less toxic Fe(III) and 
      storing iron minerals within their core. Encapsulated ferritins (EncFtn) are a 
      sub-family of ferritin-like proteins, which are widely distributed in all 
      bacterial and archaeal phyla. The recently characterized Rhodospirillum rubrum 
      EncFtn displays an unusual structure when compared with classical ferritins, with 
      an open decameric structure that is enzymatically active, but unable to store 
      iron. This EncFtn must be associated with an encapsulin nanocage in order to act 
      as an iron store. Given the wide distribution of the EncFtn family in organisms 
      with diverse environmental niches, a question arises as to whether this unusual 
      structure is conserved across the family. Here, we characterize EncFtn proteins 
      from the halophile Haliangium ochraceum and the thermophile Pyrococcus furiosus, 
      which show the conserved annular pentamer of dimers topology. Key structural 
      differences are apparent between the homologues, particularly in the centre of 
      the ring and the secondary metal-binding site, which is not conserved across the 
      homologues. Solution and native mass spectrometry analyses highlight that the 
      stability of the protein quaternary structure differs between EncFtn proteins 
      from different species. The ferroxidase activity of EncFtn proteins was 
      confirmed, and we show that while the quaternary structure around the ferroxidase 
      centre is distinct from classical ferritins, the ferroxidase activity is still 
      inhibited by Zn(II). Our results highlight the common structural organization and 
      activity of EncFtn proteins, despite diverse host environments and contexts 
      within encapsulins.
CI  - (c) 2019 The Author(s). Published by Portland Press Limited on behalf of the 
      Biochemical Society.
FAU - He, Didi
AU  - He D
AD  - Institute of Quantitative Biology, Biochemistry, and Biotechnology, School of 
      Biological Sciences, The University of Edinburgh, Max Born Crescent, Edinburgh 
      EH9 3BF, U.K.
FAU - Piergentili, Cecilia
AU  - Piergentili C
AD  - School of Natural and Environmental Sciences, Newcastle University, Newcastle 
      upon Tyne NE1 7RU, U.K.
FAU - Ross, Jennifer
AU  - Ross J
AD  - EaStCHEM School of Chemistry, The University of Edinburgh, Joseph Black Building, 
      David Brewster Road, Edinburgh EH9 3FJ, U.K.
FAU - Tarrant, Emma
AU  - Tarrant E
AD  - Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle 
      upon Tyne NE2 4HH, U.K.
FAU - Tuck, Laura R
AU  - Tuck LR
AD  - Institute of Quantitative Biology, Biochemistry, and Biotechnology, School of 
      Biological Sciences, The University of Edinburgh, Max Born Crescent, Edinburgh 
      EH9 3BF, U.K.
FAU - Mackay, C Logan
AU  - Mackay CL
AD  - EaStCHEM School of Chemistry, The University of Edinburgh, Joseph Black Building, 
      David Brewster Road, Edinburgh EH9 3FJ, U.K.
FAU - McIver, Zak
AU  - McIver Z
AD  - School of Natural and Environmental Sciences, Newcastle University, Newcastle 
      upon Tyne NE1 7RU, U.K.
FAU - Waldron, Kevin J
AU  - Waldron KJ
AUID- ORCID: 0000-0002-5577-7357
AD  - Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle 
      upon Tyne NE2 4HH, U.K.
FAU - Clarke, David J
AU  - Clarke DJ
AD  - EaStCHEM School of Chemistry, The University of Edinburgh, Joseph Black Building, 
      David Brewster Road, Edinburgh EH9 3FJ, U.K. Dave.clarke@ed.ac.uk 
      Jon.marles-wright1@ncl.ac.uk.
FAU - Marles-Wright, Jon
AU  - Marles-Wright J
AUID- ORCID: 0000-0002-9156-3284
AD  - School of Natural and Environmental Sciences, Newcastle University, Newcastle 
      upon Tyne NE1 7RU, U.K. Dave.clarke@ed.ac.uk Jon.marles-wright1@ncl.ac.uk.
LA  - eng
GR  - BB/N005570/1/BB_/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
GR  - BB/M010996/1/BB_/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
GR  - 098375/Z/12/Z/WT_/Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20190322
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Archaeal Proteins)
RN  - 0 (Bacterial Proteins)
RN  - 9007-73-2 (Ferritins)
RN  - Haliangium ochraceum
SB  - IM
MH  - Archaeal Proteins/*chemistry
MH  - Bacterial Proteins/*chemistry
MH  - Ferritins/*chemistry
MH  - Myxococcales/*chemistry
MH  - Protein Domains
MH  - Pyrococcus furiosus/*chemistry
MH  - Rhodospirillum rubrum/*chemistry
MH  - Structural Homology, Protein
MH  - Structure-Activity Relationship
OTO - NOTNLM
OT  - X-ray crystallography
OT  - encapsulated ferritin
OT  - encapsulin
OT  - ferritin
OT  - mass spectrometry
EDAT- 2019/03/07 06:00
MHDA- 2019/12/19 06:00
CRDT- 2019/03/07 06:00
PHST- 2018/12/03 00:00 [received]
PHST- 2019/02/26 00:00 [revised]
PHST- 2019/03/04 00:00 [accepted]
PHST- 2019/03/07 06:00 [pubmed]
PHST- 2019/12/19 06:00 [medline]
PHST- 2019/03/07 06:00 [entrez]
AID - BCJ20180922 [pii]
AID - 10.1042/BCJ20180922 [doi]
PST - epublish
SO  - Biochem J. 2019 Mar 22;476(6):975-989. doi: 10.1042/BCJ20180922.