Refolding and biophysical characterization of the Caulobacter crescentus copper resistance protein, PcoB: An outer membrane protein containing an intrinsically disordered domain.
Caulobacter crescentus
Copper-binding protein
Intrinsically disordered membrane protein
PcoB
Refolding
Journal
Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713
Informations de publication
Date de publication:
01 12 2022
01 12 2022
Historique:
received:
28
05
2022
revised:
16
08
2022
accepted:
25
08
2022
pubmed:
4
9
2022
medline:
7
10
2022
entrez:
3
9
2022
Statut:
ppublish
Résumé
Copper cations play fundamental roles in biological systems, such as protein folding and stabilization, or enzymatic reactions. Although copper is essential to the cell, it can become cytotoxic if present in too high concentration. Organisms have therefore developed specific regulation mechanisms towards copper. This is the case of the Pco system present in the bacterium Caulobacter crescentus, which is composed of two proteins: a soluble periplasmic protein PcoA and an outer membrane protein PcoB. PcoA oxidizes Cu
Identifiants
pubmed: 36057369
pii: S0005-2736(22)00176-6
doi: 10.1016/j.bbamem.2022.184038
pii:
doi:
Substances chimiques
Cations
0
Cations, Divalent
0
Membrane Proteins
0
Periplasmic Proteins
0
Copper
789U1901C5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
184038Informations de copyright
Copyright © 2022 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.