Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein

Publikation: Konferencebidrag › Poster › Forskning

Standard

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

Harvard

Jancsó, A, Szokolai, H, Roszahegyi, L, Szunyogh, D, Hemmingsen, LBS, Thulstrup, PW & Larsen, FH 2013, 'Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein'.

APA

Jancsó, A., Szokolai, H., Roszahegyi, L., Szunyogh, D., Hemmingsen, L. B. S., Thulstrup, P. W., & Larsen, F. H. (2013). Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein.

Vancouver

Jancsó A, Szokolai H, Roszahegyi L, Szunyogh D, Hemmingsen LBS, Thulstrup PW o.a.. Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein. 2013.

Author

Jancsó, Attila ; Szokolai, Hajnalka ; Roszahegyi, Livia ; Szunyogh, Daniel ; Hemmingsen, Lars Bo Stegeager ; Thulstrup, Peter Waaben ; Larsen, Flemming Hofmann. / Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein. 1 s.

Bibtex

@conference{ab106659a2484861bdbc3b49f4a5fabf,
title = "Metal ion interaction of an oligopeptide fragment representing the regulatory metal binding site of a CueR protein",
abstract = "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.",
author = "Attila Jancs{\'o} and Hajnalka Szokolai and Livia Roszahegyi and Daniel Szunyogh and Hemmingsen, {Lars Bo Stegeager} and Thulstrup, {Peter Waaben} and Larsen, {Flemming Hofmann}",
year = "2013",
language = "English",

}

RIS

TY - CONF

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