The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA [2]. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain [5]. [1]. 8692686. The helix-hairpin-helix DNA-binding motif: a structural basis. for non-sequence-specific recognition of DNA.. Doherty AJ, Serpell LC, Ponting CP;. Nucleic Acids Res 1996;24:2488-2497.. [2]. 8832889. Crystal structure of DNA recombination protein RuvA and a model. for its binding to the Holliday junction.. Rafferty JB, Sedelnikova SE, Hargreaves D, Artymiuk PJ, Baker. PJ, Sharples GJ, Mahdi AA, Lloyd RG, Rice DW;. Science 1996;274:415-421.. [3]. 12832627. An evolutionary analysis of the helix-hairpin-helix superfamily. of DNA repair glycosylases.. Denver DR, Swenson SL, Lynch M;. Mol Biol Evol 2003;20:1603-1611.. [4]. 10908318. Common fold in helix-hairpin-helix proteins.. Shao X, Grishin NV;. Nucleic Acids Res 2000;28:2643-2650.. [5]. 18439896. Structural biochemistry of a bacterial checkpoint protein. reveals diadenylate cyclase activity regulated by DNA. recombination intermediates.. Witte G, Hartung S, Buttner K, Hopfner KP;. Mol Cell. 2008;30:167-178. (from Pfam)
GO Terms:- Date:
- 2024-08-14