Show the
:
Protein, only.
DNA, only.
Whole complex.
Rotate
:
X 90�
X -90�
Y 90�
Y -90�
Distances
:
Central a-Helix (length in � units)
DNA, 1.5 turns (length in � units)
Reset
CRP Structure for Molecular Biology
The CRP-DNA Complex.
The
E. coli
cAMP Receptor Protein (CRP, a.k.a. CAP) is a transcriptional activator that binds to DNA (shown using the
Spacefill
display with yellow backbone). The two subunits of the symmetric dimer are shown using the
Backbone
display; the cAMP-binding domain is blue and the DNA-binding domain is purple. The cAMP molecules bound to each subunit are shown as
Spacefill
with
CPK
coloring. (
cf.
Fig. 2 of Schultz,
et al.
)
Close-up view of protein-DNA interactions in one half-site.
Amino acid sidechains H-bond to the DNA bases as follows: Arg180 to G7; Glu181 to C5; and Arg185 to G5.
The helix-turn-helix (HTH) motif is colored magenta within the purple DNA-binding domain. (
cf.
Fig. 3B of Schultz,
et al.
)
Viewing tips
:
Use the buttons to the right of the image to show only portions of the structure; then use the Chime menu to display or color the molecule. The rotate buttons act on the entire structure. Remove the distance monitors with a second click.
Go to the one-page display of one of these structures:
Back to
Structures for Molecular Biology at CMU.
The image displayed on this page requires the
Chemscape Chime
plug-in.
A description of its use at this site can be found at the
Chime Features page.
Coordinates from 1CGP.pdb.
See also Parkinson
et al.
(1996)
J. Mol. Biol.
260
395
. 1BER.pdb.
