User:David McDonald/Replication Termination Protein: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
== Structure == | == Structure == | ||
<Structure load='1BM9' size='300' frame='true' align='right' caption='RTP in solution as both a monomer and dimer' scene='Insert optional scene name here' /> | <Structure load='1BM9' size='300' frame='true' align='right' caption='1BM9: RTP in solution as both a monomer and dimer' scene='Insert optional scene name here' /> | ||
<scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_monomer/7'>RTP</scene> contains 122 amino acid residues and is an example of a winged helix structure, in the α+β protein folding family, containing four α-helices and two β-strands<sup>[1]</sup>. The structure is named a "winged helix" due to the central <scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_helical/2'>helical region</scene>, flanked by <scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_wing/2'>"wings"</scene> comprised of the two β-strands and the loops between them. | <scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_monomer/7'>RTP</scene> contains 122 amino acid residues and is an example of a winged helix structure, in the α+β protein folding family, containing four α-helices and two β-strands<sup>[1]</sup>. The structure is named a "winged helix" due to the central <scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_helical/2'>helical region</scene>, flanked by <scene name='User:David_McDonald/Replication_Termination_Protein/Rainbow_wing/2'>"wings"</scene> comprised of the two β-strands and the loops between them. | ||
| Line 30: | Line 30: | ||
== DNA Binding == | == DNA Binding == | ||
<Structure load='2EFW' size='470' frame='true' align='left' caption='RTP bound to DNA in a symmetric and asymmetric fashion' scene='Insert optional scene name here' /> | <Structure load='2EFW' size='470' frame='true' align='left' caption='2EFW: RTP bound to DNA in a symmetric and asymmetric fashion' scene='Insert optional scene name here' /> | ||
In order to terminate chromosomal replication, RTP must complex with the DNA. Two dimers of RTP bind at the Ter site, a 37bp region of DNA containing two pseudosymmetric overlapping 21 base pair half-sites A and B<sup>[3]</sup>. The B site displays significantly higher affinity for the RTP dimer<sup>[4]</sup>, however it has been shown that it is necessary for both A and B to be occupied in order for replication fork termination to occur.<sup>[4]</sup> | In order to terminate chromosomal replication, RTP must complex with the DNA. Two dimers of RTP bind at the Ter site, a 37bp region of DNA containing two pseudosymmetric overlapping 21 base pair half-sites A and B<sup>[3]</sup>. The B site displays significantly higher affinity for the RTP dimer<sup>[4]</sup>, however it has been shown that it is necessary for both A and B to be occupied in order for replication fork termination to occur.<sup>[4]</sup> | ||