Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein
Publikation: Konferencebidrag › Poster › Forskning
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Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein. / Jancsó, Attila; Szokolai, Hajnalka; Roszahegyi, Livia; Szunyogh, Daniel; Hemmingsen, Lars Bo Stegeager; Thulstrup, Peter Waaben; Larsen, Flemming Hofmann.
2013.Publikation: Konferencebidrag › Poster › Forskning
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T1 - Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein
AU - Jancsó, Attila
AU - Szokolai, Hajnalka
AU - Roszahegyi, Livia
AU - Szunyogh, Daniel
AU - Hemmingsen, Lars Bo Stegeager
AU - Thulstrup, Peter Waaben
AU - Larsen, Flemming Hofmann
PY - 2013
Y1 - 2013
N2 - Metalloregulatory proteins of the MerR family are transcriptional activatorsthat sense/control the concentration of various metal ions inside bacteria.1The Cu+ efflux regulator CueR, similarly to other MerR proteins, possesses ashort multiple Cys-containing metal binding loop close to the C-terminus.CueR has a high selectivity for Cu+, Ag+ and Au+, but exhibits notranscriptional activity for the divalent ions Hg2+ and Zn2+.2 The two Cys-residues of the metal binding loop were shown to settle M+ ions into a linearcoordination environment but other factors may also play a role in therecognition of cognate metal ions.2 Nevertheless, it is an interesting questionwhether the same sequence, when removed from the protein, shows aflexibility to adopt different coordination environments and may efficientlybind metal ions having preferences for larger coordination numbers.
AB - Metalloregulatory proteins of the MerR family are transcriptional activatorsthat sense/control the concentration of various metal ions inside bacteria.1The Cu+ efflux regulator CueR, similarly to other MerR proteins, possesses ashort multiple Cys-containing metal binding loop close to the C-terminus.CueR has a high selectivity for Cu+, Ag+ and Au+, but exhibits notranscriptional activity for the divalent ions Hg2+ and Zn2+.2 The two Cys-residues of the metal binding loop were shown to settle M+ ions into a linearcoordination environment but other factors may also play a role in therecognition of cognate metal ions.2 Nevertheless, it is an interesting questionwhether the same sequence, when removed from the protein, shows aflexibility to adopt different coordination environments and may efficientlybind metal ions having preferences for larger coordination numbers.
M3 - Poster
ER -
ID: 48680773