Beyond copper: examining the significance of His-mutations in mycobacterial GroEL1 HRCT for Ni(II) complex stability and formation.


Journal

Dalton transactions (Cambridge, England : 2003)
ISSN: 1477-9234
Titre abrégé: Dalton Trans
Pays: England
ID NLM: 101176026

Informations de publication

Date de publication:
25 Mar 2024
Historique:
medline: 25 3 2024
pubmed: 25 3 2024
entrez: 25 3 2024
Statut: aheadofprint

Résumé

Recently, we have studied the coordination chemistry of the Cu(II)-histidine-rich C-terminal tail (HRCT) complex of the mycobacterial GroEL1 protein. The structure of this domain differs significantly compared to the well-known methionine-glycine-rich GroEL chaperonin - it was predicted that mycobacterial GroEL1 could play a significant role in the metal homeostasis of

Identifiants

pubmed: 38526845
doi: 10.1039/d4dt00011k
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Auteurs

Anna Rola (A)

Faculty of Chemistry, University of Wroclaw, 50- 383 Wroclaw, Poland. slawomir.potocki@uwr.edu.pl.

Arian Kola (A)

Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A. Moro 2, 53100 Siena, Italy.

Daniela Valensin (D)

Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A. Moro 2, 53100 Siena, Italy.

Oscar Palacios (O)

Departament de Química, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallès, Spain.

Merce Capdevila (M)

Departament de Química, Universitat Autònoma de Barcelona, 08193 Cerdanyola del Vallès, Spain.

Elżbieta Gumienna-Kontecka (E)

Faculty of Chemistry, University of Wroclaw, 50- 383 Wroclaw, Poland. slawomir.potocki@uwr.edu.pl.

Sławomir Potocki (S)

Faculty of Chemistry, University of Wroclaw, 50- 383 Wroclaw, Poland. slawomir.potocki@uwr.edu.pl.

Classifications MeSH