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MerR family transcriptional regulator
MerR family DNA-binding protein
Members of this family of DNA-binding domains are predominantly found in the prokaryotic transcriptional regulator MerR. They adopt a structure consisting of a core of three alpha helices, with an architecture that is similar to that of the 'winged helix' fold [1]. [1]. 12958362. Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR. Changela A, Chen K, Xue Y, Holschen J, Outten CE, O'Halloran TV, Mondragon A;. Science. 2003;301:1383-1387. (from Pfam)
MerR family DNA-binding transcriptional regulator
Cu(I)-responsive transcriptional regulator
This HMM represents the copper-, silver- and gold- (I) responsive transcriptional activator of the gamma proteobacterial copper efflux system [1]. This protein is a member of the MerR family of transcriptional activators (PF00376) and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X7-Cys. This family also lacks a conserved cysteine at the N-terminal end of the dimerization helix which is required for the binding of divalent metals such as zinc; here it is replaced by a serine residue [2].
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