Sandbox20: Difference between revisions

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=== Replication Termination Activity===
=== Replication Termination Activity===


The consequence of these different conformations is most prominent in the position of the B1 sheet. This is evident in the Tyr33 residue, <scene name='Sandbox20/2efw/20'>shown by clicking here</scene>
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>
Space, which contact DNA only in the wing-down conformation.
 
Herman's:
The asymmetric arrangement of the RTP dimer means that certain regions of the protein are accessible from one face only. In particular, Y33 in the wing-down monomer always comes in contact with the replication fork that is arrested. Of interest is that Y33 is found in a region that carries some similarity to DnaB, and this region is believed to interact with DnaB, likely in combination with the adjacent hydrophobic patch, in order to suppress its helicase activity.* At the moment, it is unclear why, but both the TerA and TerB sites must be occupied for full replication termination activity. (Reference??)
 
*1bm9 paper


==Tus==
==Tus==