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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
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Coordinates from 1CGP.pdb.
See also Parkinson
et al.
(1996)
J. Mol. Biol.
260
395
. 1BER.pdb.
