Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
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 protein may bind DNA and function as a transcriptional regulator, similar to Caulobacter vibrioides orphan antitoxin ParD2, the antitoxin component of a non-functional type II toxin-antitoxin
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on