An EPR Study on the Interaction between the Cu(I) Metal Binding Domains of ATP7B and the Atox1 Metallochaperone.
ATP7B
Atox1
DEER
EPR
copper metabolism
metal binding domains
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
02 Aug 2020
02 Aug 2020
Historique:
received:
19
07
2020
revised:
29
07
2020
accepted:
30
07
2020
entrez:
5
8
2020
pubmed:
5
8
2020
medline:
23
2
2021
Statut:
epublish
Résumé
Copper's essentiality and toxicity mean it requires a sophisticated regulation system for its acquisition, cellular distribution and excretion, which until now has remained elusive. Herein, we applied continuous wave (CW) and pulsed electron paramagnetic resonance (EPR) spectroscopy in solution to resolve the copper trafficking mechanism in humans, by considering the route travelled by Cu(I) from the metallochaperone Atox1 to the metal binding domains of ATP7B. Our study revealed that Cu(I) is most likely mediated by the binding of the Atox1 monomer to metal binding domain 1 (MBD1) and MBD4 of ATP7B in the final part of its extraction pathway, while the other MBDs mediate this interaction and participate in copper transfer between the various MBDs to the ATP7B membrane domain. This research also proposes that MBD1-3 and MBD4-6 act as two independent units.
Identifiants
pubmed: 32748830
pii: ijms21155536
doi: 10.3390/ijms21155536
pmc: PMC7432781
pii:
doi:
Substances chimiques
ATOX1 protein, human
0
Copper Transport Proteins
0
Molecular Chaperones
0
Copper
789U1901C5
Copper-Transporting ATPases
EC 7.2.2.8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : European Research Council
ID : 754365
Pays : International
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