Rtp and Tus DNA Binding

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Assymmetry of RTP in DNA-binding
Assymmetry of RTP in DNA-binding
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Wing-up <scene name='Rtp_and_Tus_DNA_Binding/Wingup/1'>(green)</scene>: Contacts upstream with rtp dimer bound to A-site
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<scene name='Rtp_and_Tus_DNA_Binding/Wingup/1'>Wing-up</scene>: Contacts upstream with rtp dimer bound to A-site
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Wing-down <scene name='Rtp_and_Tus_DNA_Binding/Wingdown/1'>(blue)</scene>: Contacts with phosphate backbone of downstream DNA
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<scene name='Rtp_and_Tus_DNA_Binding/Wingdown/1'>Wing-down</scene>: Contacts with phosphate backbone of downstream DNA
<scene name='Rtp_and_Tus_DNA_Binding/Overview/1'>Overview</scene>
<scene name='Rtp_and_Tus_DNA_Binding/Overview/1'>Overview</scene>

Revision as of 03:18, 23 May 2011

Replication Termination Proteins

Rtp and Tus These polar fork bocking sites have been found in yeast, pea, frog and human genomes.

RTP

RTP is a DNA binding protein from Bacillus Subtilis that uses a helix-loop-helix binding motif. In solution it shows a symmetric structure typical of the winged helix loop helix family, with an unstructured end, first alpha helix , unstructured loop that is equivalent to the first beta sheet , helix loop helix structure (-), 2 beta sheets with a connecting loop that makes up the 'wing' structure and an additional long alpha helix involved in dimerisation .

Assymmetry of RTP in DNA-binding : Contacts upstream with rtp dimer bound to A-site : Contacts with phosphate backbone of downstream DNA


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Proteopedia Page Contributors and Editors (what is this?)

Craig Mooney, Michal Harel

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