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

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Tying Up a Loose End : On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR. / Balogh, Ria K.; Gyurcsik, Bela; Jensen, Mikael; Thulstrup, Peter W.; Koester, Ulli; Christensen, Niels Johan; Jensen, Marianne L.; Hunyadi-Gulyas, Eva; Hemmingsen, Lars; Jancso, Attila.

I: ChemBioChem, Bind 23, Nr. 16, 202200290, 2022.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Balogh, RK, Gyurcsik, B, Jensen, M, Thulstrup, PW, Koester, U, Christensen, NJ, Jensen, ML, Hunyadi-Gulyas, E, Hemmingsen, L & Jancso, A 2022, 'Tying Up a Loose End: On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR', ChemBioChem, bind 23, nr. 16, 202200290. https://doi.org/10.1002/cbic.202200290

APA

Balogh, R. K., Gyurcsik, B., Jensen, M., Thulstrup, P. W., Koester, U., Christensen, N. J., Jensen, M. L., Hunyadi-Gulyas, E., Hemmingsen, L., & Jancso, A. (2022). Tying Up a Loose End: On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR. ChemBioChem, 23(16), [202200290]. https://doi.org/10.1002/cbic.202200290

Vancouver

Balogh RK, Gyurcsik B, Jensen M, Thulstrup PW, Koester U, Christensen NJ o.a. Tying Up a Loose End: On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR. ChemBioChem. 2022;23(16). 202200290. https://doi.org/10.1002/cbic.202200290

Author

Balogh, Ria K. ; Gyurcsik, Bela ; Jensen, Mikael ; Thulstrup, Peter W. ; Koester, Ulli ; Christensen, Niels Johan ; Jensen, Marianne L. ; Hunyadi-Gulyas, Eva ; Hemmingsen, Lars ; Jancso, Attila. / Tying Up a Loose End : On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR. I: ChemBioChem. 2022 ; Bind 23, Nr. 16.

Bibtex

@article{3b3b78961bed4e19b0daab75925715df,
title = "Tying Up a Loose End: On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR",
abstract = "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 Delta 7C-CueR.([111) Ag PAC spectroscopy demonstrates that the WT-CueR metal site structure (AgS2) 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.",
keywords = "metalloproteins, metalloregulatory proteins, protein metal site structures, silver, thiolate coordination, MERR FAMILY, ESCHERICHIA-COLI, METAL-IONS, BINDING, ACTIVATION, SILVER",
author = "Balogh, {Ria K.} and Bela Gyurcsik and Mikael Jensen and Thulstrup, {Peter W.} and Ulli Koester and Christensen, {Niels Johan} and Jensen, {Marianne L.} and Eva Hunyadi-Gulyas and Lars Hemmingsen and Attila Jancso",
year = "2022",
doi = "10.1002/cbic.202200290",
language = "English",
volume = "23",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "16",

}

RIS

TY - JOUR

T1 - Tying Up a Loose End

T2 - On the Role of the C-Terminal CCHHRAG Fragment of the Metalloregulator CueR

AU - Balogh, Ria K.

AU - Gyurcsik, Bela

AU - Jensen, Mikael

AU - Thulstrup, Peter W.

AU - Koester, Ulli

AU - Christensen, Niels Johan

AU - Jensen, Marianne L.

AU - Hunyadi-Gulyas, Eva

AU - Hemmingsen, Lars

AU - Jancso, Attila

PY - 2022

Y1 - 2022

N2 - 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 Delta 7C-CueR.([111) Ag PAC spectroscopy demonstrates that the WT-CueR metal site structure (AgS2) 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.

AB - 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 Delta 7C-CueR.([111) Ag PAC spectroscopy demonstrates that the WT-CueR metal site structure (AgS2) 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.

KW - metalloproteins

KW - metalloregulatory proteins

KW - protein metal site structures

KW - silver

KW - thiolate coordination

KW - MERR FAMILY

KW - ESCHERICHIA-COLI

KW - METAL-IONS

KW - BINDING

KW - ACTIVATION

KW - SILVER

U2 - 10.1002/cbic.202200290

DO - 10.1002/cbic.202200290

M3 - Journal article

C2 - 35714117

VL - 23

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 16

M1 - 202200290

ER -

ID: 313053558