Structures Generated at SMRL

5 Space filling models of the trp repressor-mtr DNA solution complex mean structures.
The model is rotated from (a) 0 degree to (b)45 to (c) 90 to (d) 135 to (e) 180 degrees. The mtr DNA molecule is shown in pale pink, the cofactor L-tryptophan molecules in red, monomer I (except the D and E helix regions) in yellow, monomer II (except the D and E helix regions) in purple, the D helix regions in green (the upper green atoms belong to monomer I and the lower to monomer II) and the E helix regions in orange (the upper orange atoms belong to monomer I and the lower to monomer II).

Trp Repressor Binding Region
Rasmol model of trp repressor showing location of helices A, B, C, D, E, and F within the homodimer, with the DNA-binding region in red and the N-terminal region in yellow. Finucane and Jardetzky (1995) J. Mol. Biol. 253, 576-589.


Inline Graphic Image of the trp repressor complexed with DNA operator concensus sequence.

Trp Repressor and DNA "Shaking Hands"
This graphic represents the structure of trp- repressor bound to DNA as determined from NMR data. Structurally, trp- repressor is a symmetric dimer, a molecule formed of two identical subunits (light blue and pink) intertwined with each other. The red atoms represent the two tryptophan ligands, molecules that bind with the represssor before it binds with DNA (light green).

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