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ribbon-helix-helix protein, CopG family
The structure of this protein repressor, which is the shortest reported to date and the first isolated from a plasmid, has a homodimeric ribbon-helix-helix arrangement [2]. The helix-turn-helix-like structure is involved in dimerisation and not DNA binding as might have been expected [2]. [1]. 9714164. Structural features of the plasmid pMV158-encoded. transcriptional repressor CopG, a protein sharing similarities. with both helix-turn-helix and beta-sheet DNA binding proteins.. Acebo P, Garcia de Lacoba M, Rivas G, Andreu JM, Espinosa M, del. Solar G. Proteins 1998;32:248-261.. [2]. 9857196. The structure of plasmid-encoded transcriptional repressor CopG. unliganded and bound to its operator.. Gomis-R th FX, Sol M, Acebo P, Parraga A, Guasch A, Eritja R,. Gonzalez A, Espinosa M, del Solar G, Coll M. EMBO J 1998;17:7404-7415. (from Pfam)
CopG family ribbon-helix-helix protein
CopG family ribbon-helix-helix (RHH) protein similar to CopG/NikR family transcriptional regulators and to Bacillus subtilis antitoxin EndoAI (MazE), which inactivates the toxin EndoA (MazF), an mRNA interferase that cleaves mRNAs in a sequence-specific manner, resulting in cellular growth arrest
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