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===Structural Overview===
===Structural Overview===
[[Image:RTP 1 Symmetry.jpg | thumb | upright=1.4| left| The two subunits of the RTP dimer complex.]]
The structure of an RTP monomer bears greatest similarity to the "''classic winged-helix''" motif, where 'wings' project from the loop between the final two β sheets of a compact αβααββ structure. The two major variations from this theme are the absence of a β1 sheet (the corresponding region is termed the β1 loop), and the presence of a fourth elongate α-helix, which facilitates dimerisation. Each of these secondary structural elements are indicated in the structure <scene name='Sandbox20/2efw/8'>shown here</scene>.
The structure of an RTP monomer bears greatest similarity to the "''classic winged-helix''" motif, where 'wings' project from the loop between the final two β sheets of a compact αβααββ structure. The two major variations from this theme are the absence of a β1 sheet (the corresponding region is termed the β1 loop), and the presence of a fourth elongate α-helix, which facilitates dimerisation. Each of these secondary structural elements are indicated in the structure <scene name='Sandbox20/2efw/8'>shown here</scene>.


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13-15 residues contribute to the attachment of an RTP molecule to the ''Ter'' DNA site. Most of this is contributed by the basic residues of the <scene name='Sandbox20/2efw/30'>α3 helix</scene>, which lies in the major groove of DNA.  
13-15 residues contribute to the attachment of an RTP molecule to the ''Ter'' DNA site. Most of this is contributed by the basic residues of the <scene name='Sandbox20/2efw/30'>α3 helix</scene>, which lies in the major groove of DNA.  


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

Student, Craig T Martin, Michael Webster