Rtp and Tus DNA Binding: Difference between revisions

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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 <scene name='Rtp_and_Tus_DNA_Binding/Nterm/1'>N-terminus</scene> end, first alpha helix <scene name='Rtp_and_Tus_DNA_Binding/Alpha1/1'>(a1)</scene>, unstructured loop that is equivalent to the first beta sheet <scene name='Rtp_and_Tus_DNA_Binding/Beta1/1'>(B1)</scene>, helix loop helix structure (<scene name='Rtp_and_Tus_DNA_Binding/Alpha2/1'>a2</scene>-<scene name='Rtp_and_Tus_DNA_Binding/Alpha3/1'>a3</scene>), 2 beta sheets with a connecting loop that makes up the 'wing' structure <scene name='Rtp_and_Tus_DNA_Binding/Wing/1'>(B2 - B3)</scene> and an additional long alpha helix involved in dimerisation <scene name='Rtp_and_Tus_DNA_Binding/Alpha4/1'>(a4)</scene>.
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 <scene name='Rtp_and_Tus_DNA_Binding/Nterm/1'>N-terminus</scene> end, first alpha helix <scene name='Rtp_and_Tus_DNA_Binding/Alpha1/1'>(a1)</scene>, unstructured loop that is equivalent to the first beta sheet <scene name='Rtp_and_Tus_DNA_Binding/Beta1/1'>(B1)</scene>, helix loop helix structure (<scene name='Rtp_and_Tus_DNA_Binding/Alpha2/1'>a2</scene>-<scene name='Rtp_and_Tus_DNA_Binding/Alpha3/1'>a3</scene>), 2 beta sheets with a connecting loop that makes up the 'wing' structure <scene name='Rtp_and_Tus_DNA_Binding/Wing/1'>(B2 - B3)</scene> and an additional long alpha helix involved in dimerisation <scene name='Rtp_and_Tus_DNA_Binding/Alpha4/1'>(a4)</scene>.


 
Assymmetry of RTP in DNA-binding
 
Wing-up <scene name='Rtp_and_Tus_DNA_Binding/Wingup/1'>(green)</scene>: Contacts upstream with rtp dimer bound to A-site
The RTP binding site consists of a 30bp sequence consisting of two inperfect 16 bp repeats, the A site and the B site.
Wing-down <scene name='Rtp_and_Tus_DNA_Binding/Wingdown/1'>(blue)</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 06:17, 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 Wing-up : Contacts upstream with rtp dimer bound to A-site Wing-down : Contacts with phosphate backbone of downstream DNA


Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Craig Mooney, Michal Harel