Sandbox20: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Student, Craig T Martin, Michael Webster

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 [[Image:Tus 2 DNA-binding domain.jpg | thumb | upright=1.4| left| Interaction between the beta sheet domain of Tus and the TerB DNA region.]]
+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.
-Tus is among the most stable monomeric, sequence-specific, double-stranded DNA-binding proteins. Three major sets of interactions contribute to this; (1) the phosphate clamp within the amino domain, (2) base-specific polar interactions by the β-sheet within the major groove, and (3) non-polar contacts within the carboxy domain.
+. Interaction between the three β-sheets and the major groove of DNA involves both base-specific and base non-specific bonds.
+(<scene name='Sandbox20/Tus/19'>shown here</scene>).
-. Interaction between beta sheets (shown in green) and the major groove of DNA (<scene name='Sandbox20/Tus/19'>shown here</scene>).
+.
+. The phosphate clamp is located at the end of the aIV and aV helices, closest to where the replication fork is stalled. <ref>pdb:  8857533</ref> It ensures the protein does not come loose at the critical end and allow helicase activity to occur. It involves five, mostly van der Waals, contacts with the sugar-phosphate backbone.
 ===Replication Termination Activity===