Dissecting the structural and functional roles of a putative metal entry site in encapsulated ferritins.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
13 11 2020
Historique:
received: 25 05 2020
revised: 24 08 2020
pubmed: 4 9 2020
medline: 10 3 2021
entrez: 4 9 2020
Statut: ppublish

Résumé

Encapsulated ferritins belong to the universally distributed ferritin superfamily, whose members function as iron detoxification and storage systems. Encapsulated ferritins have a distinct annular structure and must associate with an encapsulin nanocage to form a competent iron store that is capable of holding significantly more iron than classical ferritins. The catalytic mechanism of iron oxidation in the ferritin family is still an open question because of the differences in organization of the ferroxidase catalytic site and neighboring secondary metal-binding sites. We have previously identified a putative metal-binding site on the inner surface of the

Identifiants

pubmed: 32878987
pii: S0021-9258(17)50385-3
doi: 10.1074/jbc.RA120.014502
pmc: PMC7667983
pii:
doi:

Substances chimiques

Bacterial Proteins 0
Metals 0
Recombinant Proteins 0
Iron E1UOL152H7
Ceruloplasmin EC 1.16.3.1
Zinc J41CSQ7QDS

Banques de données

PDB
['5DA5']
figshare
['10.6084/m9.figshare.11920512']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

15511-15526

Subventions

Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/N005570/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/M010996/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 098375/Z/12/Z
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R013942/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R013993/1
Pays : United Kingdom

Informations de copyright

© 2020 Piergentili et al.

Déclaration de conflit d'intérêts

Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.

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Auteurs

Cecilia Piergentili (C)

School of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom.

Jennifer Ross (J)

EaStCHEM School of Chemistry, University of Edinburgh, Edinburgh, Scotland.

Didi He (D)

Institute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, Scotland.

Kelly J Gallagher (KJ)

EaStCHEM School of Chemistry, University of Edinburgh, Edinburgh, Scotland.

Will A Stanley (WA)

School of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom.

Laurène Adam (L)

School of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom.

C Logan Mackay (CL)

EaStCHEM School of Chemistry, University of Edinburgh, Edinburgh, Scotland.

Arnaud Baslé (A)

Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom.

Kevin J Waldron (KJ)

Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom.

David J Clarke (DJ)

EaStCHEM School of Chemistry, University of Edinburgh, Edinburgh, Scotland. Electronic address: Dave.clarke@ed.ac.uk.

Jon Marles-Wright (J)

School of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom. Electronic address: Jon.marles-wright1@ncl.ac.uk.

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Classifications MeSH