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)
GO Terms:- Biological Process:
- regulation of DNA-templated transcription (GO:0006355)
- Date:
- 2024-04-03