Sandbox20: Difference between revisions

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===DNA Binding===
===DNA Binding===
[[Image:Tus 2 DNA-binding domain.jpg | thumb | upright=1.4| right| 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. 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.


1. Interaction between the three β-sheets and the major groove of DNA involves both base-specific and base non-specific bonds.  
1. 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>).
(<scene name='Sandbox20/Tus/19'>shown here</scene>).
{|
| [[Image:Tus 2 DNA-binding domain.jpg|thumb|upright=1.3|Interaction between the beta sheet domain of Tus and the TerB DNA region.]]
| [[Image:Tus-DNA polar contacts.jpg|thumb|upright|Base-specific polar contacts between the βJ strand and the major DNA groove.]]
| [[Image:Tus-DNA nonpolar contacts.jpg|thumb|upright=1.4|Van der Waals and hydrophobic interactions between the βJ strand and the major DNA groove.]]
|}
2.  
2.  
3. 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.
3. 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.

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

Student, Craig T Martin, Michael Webster