ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins
This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.
Comment:the ribbon-helix-helix (RHH) type DNA-binding motif dimerizes as two antiparallel beta-strands which compose a ribbon; the beta-strands are involved both in dimer formation and in specific interactions with the DNA by fitting snugly into the major groove
Structure:1B01: Streptococcus agalactiae transcriptional repressor CopG forms a homodimer; contacts at 4.0A - View structure with Cn3D
Structure:2RBF: Escherichia coli proline utilization A (PutA) ribbon-helix-helix domain (PutA52) forms a homodimer; contacts at 4.0A - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",