Sandbox20: Difference between revisions

Tus is among the most stable monomeric, sequence-specific, double-stranded DNA-binding proteins. This is due to a combination of three major sets of interactions; base-specific polar interactions within the major groove, non-polar contacts with the carboxy domain, and a phosphate clamp within the amino domain. The three β-sheets which span the major groove of DNA make both base-specific and base non-specific bonds, as shown in <scenename='Sandbox20/Tus/19'>this model</scene>. In particular, three glutamine residues on the βJ strand form bidentate hydrogen bonds to bases at the permissive end of the complex (below centre). Interspersed with these residues on the same strand, residues such as isoleucine make Van der Waals and hydrophobic interactions to sugar and base moieties (below right).