Rtp and Tus DNA Binding: Difference between revisions
Craig Mooney (talk | contribs) No edit summary |
Craig Mooney (talk | contribs) No edit summary |
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Assymmetry of RTP in DNA-binding | Assymmetry of RTP in DNA-binding | ||
<scene name='Rtp_and_Tus_DNA_Binding/Wingup/1'>Wing-up</scene>: Contacts upstream with rtp dimer bound to A-site | |||
<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 N-terminus end, first alpha helix (a1), unstructured loop that is equivalent to the first beta sheet (B1), helix loop helix structure (a2-a3), 2 beta sheets with a connecting loop that makes up the 'wing' structure (B2 - B3) and an additional long alpha helix involved in dimerisation (a4).
Assymmetry of RTP in DNA-binding Wing-up: Contacts upstream with rtp dimer bound to A-site Wing-down: Contacts with phosphate backbone of downstream DNA
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