Rtp and Tus DNA Binding: Difference between revisions
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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/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/Wingdown/1'>Wing-down</scene>: Contacts with phosphate backbone of downstream DNA | ||
Residues binding to DNA | |||
<Structure load='Lol1.pdb' size='400' color='white'/> | <Structure load='Lol1.pdb' size='400' color='white'/> | ||
Revision as of 06:24, 23 May 2011
Replication Termination ProteinsReplication Termination Proteins
Rtp and Tus These polar fork bocking sites have been found in yeast, pea, frog and human genomes.
RTPRTP
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
Residues binding to DNA
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