Sandbox20: Difference between revisions
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The asymmetric arrangement of the RTP dimer means that certain regions of the protein are accessible from one face only. In particular, Tyr33 makes contact with the replication fork in the wing-down monomer only, as shown in this <scene name='Sandbox20/2efw/20'>model</scene>. Interestingly, residues in proximity to Tyr33 carry similarity to those of the leading face of DnaB helicase, suggesting some direct interaction. This may contribute to the suppression of helicase activity <ref>pdb: 7867072</ref>. For unknown reasons, both the TerA and TerB sites must be occupied for full replication termination activity. <ref>pdb: 17521668</ref> | The asymmetric arrangement of the RTP dimer means that certain regions of the protein are accessible from one face only. In particular, Tyr33 makes contact with the replication fork in the wing-down monomer only, as shown in this <scene name='Sandbox20/2efw/20'>model</scene>. Interestingly, residues in proximity to Tyr33 carry similarity to those of the leading face of DnaB helicase, suggesting some direct interaction. This may contribute to the suppression of helicase activity <ref>pdb: 7867072</ref>. For unknown reasons, both the TerA and TerB sites must be occupied for full replication termination activity. <ref>pdb: 17521668</ref> | ||
Index of RTP scenes:<scene name='Sandbox20/2efw/8'>secondary structures</scene>, <scene name='Sandbox20/2efw/14'>DNA-binding</scene>, <scene name='Sandbox20/2efw/20'>dimer asymmetry</scene>. | |||
==Tus== | ==Tus== | ||
