Tying Up a Loose End: On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR.

Autor: Balogh RK; Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary., Gyurcsik B; Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary., Jensen M; Hevesy Laboratory, Department of Health Technology, Technical University of Denmark, Frederiksborgvej 399, 4000, Roskilde, Denmark., Thulstrup PW; Department of Chemistry, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen, Denmark., Köster U; Institut Laue-Langevin, 71 avenue des Martyrs, 38042, Grenoble, France., Christensen NJ; Department of Chemistry, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg C, Denmark., Jensen ML; Niels Bohr Institute, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen, Denmark., Hunyadi-Gulyás É; Laboratory of Proteomics Research, Biological Research Centre, Eötvös Loránd Research Network, Temesvári krt. 62, 6726, Szeged, Hungary., Hemmingsen L; Department of Chemistry, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen, Denmark., Jancsó A; Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2022 Aug 17; Vol. 23 (16), pp. e202200290. Date of Electronic Publication: 2022 Jul 05.
DOI: 10.1002/cbic.202200290
Abstrakt: The transcriptional regulator CueR is activated by the binding of Cu I , Ag I , or Au I to two cysteinates in a near-linear fashion. The C-terminal CCHHRAG sequence in Escherichia coli CueR present potential additional metal binding ligands and here we explore the effect of deleting this fragment on the binding of Ag I to CueR. CD spectroscopic and ESI-MS data indicate that the high Ag I -binding affinity of WT-CueR is significantly reduced in Δ7C-CueR. [111 Ag PAC spectroscopy demonstrates that the WT-CueR metal site structure (AgS 2 ) is conserved, but less populated in the truncated variant. Thus, the function of the C-terminal fragment may be to stabilize the two-coordinate metal site for cognate monovalent metal ions. In a broader perspective this is an example of residues beyond the second coordination sphere affecting metal site physicochemical properties while leaving the structure unperturbed.
(© 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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