User:David McDonald/Replication Termination Protein: Difference between revisions

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The observed symmetry was in contrast to the known polarity of the RTP-Ter site. Further research using the wild-type Ter sequence (nRB) revealed a distinct <scene name='User:David_McDonald/Replication_Termination_Protein/Asymmetric_binding/4'>Asymmetry</scene> in both the RTP dimer and the DNA[3]. Although the interacting sequences remained the same, the downstream monomer displayed a <scene name='User:David_McDonald/Replication_Termination_Protein/Asymmetric_down/2'>"Wing down"</scene> confirmation, where the β2-loop-β3 structure makes contact with the phosphate backbone. Conversely, the upstream monomer displays a <scene name='User:David_McDonald/Replication_Termination_Protein/Asymmetric_up/2'>"Wing up"</scene> confirmation, with the wing making contact with the upstream minor groove.
The observed symmetry was in contrast to the known polarity of the RTP-Ter site. Further research using the wild-type Ter sequence (nRB) revealed a distinct <scene name='User:David_McDonald/Replication_Termination_Protein/Asymmetric_binding/4'>Asymmetry</scene> in both the RTP dimer and the DNA[3]. Although the interacting sequences remained the same, the downstream monomer displayed a <scene name='User:David_McDonald/Replication_Termination_Protein/Asymmetric_down/2'>"Wing down"</scene> confirmation, where the β2-loop-β3 structure makes contact with the phosphate backbone. Conversely, the upstream monomer displays a <scene name='User:David_McDonald/Replication_Termination_Protein/Asymmetric_up/2'>"Wing up"</scene> confirmation, with the wing making contact with the upstream minor groove.




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