Sandbox20: Difference between revisions
From Proteopedia
Jump to navigationJump to search
| Line 25: | Line 25: | ||
===Structural Overview=== | ===Structural Overview=== | ||
[[Image:RTP 1 Symmetry.jpg | thumb | upright=1. | [[Image:RTP 1 Symmetry.jpg | thumb | upright=1.3| left| The two subunits of the RTP dimer complex.]] [[Image:RTP Dimerisation.jpg | thumb | upright=1.2| right| Interactions between a4 helices facilitates dimerisation of RTP on the Ter DNA site.]] | ||
The structure of an RTP monomer bears greatest similarity to the "''classic winged-helix''" motif, in which '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 instead 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>. | |||
===DNA Binding=== | ===DNA Binding=== | ||
