Replication Termination Protein: Difference between revisions

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==RTP Structure==
==RTP Structure==


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='44/449701/1/3'>N-terminus</scene> end, first alpha helix <scene name='44/449701/1/4'>(a1)</scene>, unstructured loop that is equivalent to the first beta sheet <scene name='44/449701/1/6'>(B1)</scene>, helix loop helix structure (<scene name='44/449701/1/5'>a2</scene>-<scene name='44/449701/1/7'>a3</scene>), 2 beta sheets with a connecting loop that makes up the 'wing' structure <scene name='44/449701/1/8'>(B2 - B3)</scene> and an additional long alpha helix involved in dimerisation <scene name='Rtp_and_Tus_DNA_Binding/Alpha4/1'>(a4)</scene>.<ref>Vivian JP, Porter CJ, Wilce JA, Wilce MCJ, (2007) An asymmetric structure of the Bacillus subtilise Replication Terminator Protein in Complex with DNA. J. Mol. Bio, 370:481-491</ref>
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='44/449701/1/3'>N-terminus</scene> end, first alpha helix <scene name='44/449701/1/4'>(a1)</scene>, unstructured loop that is equivalent to the first beta sheet <scene name='44/449701/1/6'>(B1)</scene>, helix loop helix structure (<scene name='44/449701/1/5'>a2</scene>-<scene name='44/449701/1/7'>a3</scene>), 2 beta sheets with a connecting loop that makes up the 'wing' structure <scene name='44/449701/1/8'>(B2 - B3)</scene> and an additional long alpha helix involved in dimerisation <scene name='44/449701/1/9'>(a4)</scene>.<ref>Vivian JP, Porter CJ, Wilce JA, Wilce MCJ, (2007) An asymmetric structure of the Bacillus subtilise Replication Terminator Protein in Complex with DNA. J. Mol. Bio, 370:481-491</ref>


Binding of Rtp to the assymetric B portion of the Ter site changes its conformation into an assymetric 'wing-up wing-down' structure.
Binding of Rtp to the assymetric B portion of the Ter site changes its conformation into an assymetric 'wing-up wing-down' structure.