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
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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
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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