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

Publikation: ForskningPoster

Dokumenter

Attila Jancsó, Hajnalka Szokolai, Livia Roszahegyi, Daniel Szunyogh, Lars Bo Stegeager Hemmingsen, Peter Waaben Thulstrup, Flemming Hofmann Larsen

Metalloregulatory proteins of the MerR family are transcriptional activators
that sense/control the concentration of various metal ions inside bacteria.1
The Cu+ efflux regulator CueR, similarly to other MerR proteins, possesses a
short multiple Cys-containing metal binding loop close to the C-terminus.
CueR has a high selectivity for Cu+, Ag+ and Au+, but exhibits no
transcriptional 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 linear
coordination environment but other factors may also play a role in the
recognition of cognate metal ions.2 Nevertheless, it is an interesting question
whether the same sequence, when removed from the protein, shows a
flexibility to adopt different coordination environments and may efficiently
bind metal ions having preferences for larger coordination numbers.
OriginalsprogEngelsk
Publikationsdato2013
Antal sider1
StatusUdgivet - 2013

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