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PDBsum entry 1u3c
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Signaling protein
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PDB id
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1u3c
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of the photolyase-Like domain of cryptochrome 1 from arabidopsis thaliana.
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Authors
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C.A.Brautigam,
B.S.Smith,
Z.Ma,
M.Palnitkar,
D.R.Tomchick,
M.Machius,
J.Deisenhofer.
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Ref.
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Proc Natl Acad Sci U S A, 2004,
101,
12142-12147.
[DOI no: ]
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PubMed id
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Abstract
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Signals generated by cryptochrome (CRY) blue-light photoreceptors are
responsible for a variety of developmental and circadian responses in plants.
The CRYs are also identified as circadian blue-light photoreceptors in
Drosophila and components of the mammalian circadian clock. These flavoproteins
all have an N-terminal domain that is similar to photolyase, and most have an
additional C-terminal domain of variable length. We present here the crystal
structure of the photolyase-like domain of CRY-1 from Arabidopsis thaliana. The
structure reveals a fold that is very similar to photolyase, with a single
molecule of FAD noncovalently bound to the protein. The surface features of the
protein and the dissimilarity of a surface cavity to that of photolyase account
for its lack of DNA-repair activity. Previous in vitro experiments established
that the photolyase-like domain of CRY-1 can bind Mg.ATP, and we observe a
single molecule of an ATP analog bound in the aforementioned surface cavity,
near the bound FAD cofactor. The structure has implications for the signaling
mechanism of CRY blue-light photoreceptors.
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Figure 1.
Fig. 1. Structure of CRY1-PHR and its disulfide bond. (A)
The structure of CRY1-PHR. Green, helices; purple,  -strands;
dark blue, loop regions; orange, FAD cofactor; light blue,
AMP-PNP, which is not bound in the native structure. (B) The
disulfide bond in CRY1-PHR. The side chains of Cys-80 and
Cys-190 are shown, with the carbons in dark blue and the sulfurs
in yellow. Superimposed is a simulated-annealing omit map (F[o]
- F[c], contoured at 3  ) (28). Figs. 1 and 3
were generated by using PYMOL.
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Figure 2.
Fig. 2. Surface features near to the FAD-access cavity.
Shown are the surfaces of CRY1-PHR (A) and photolyase (B). The
electrostatic potential is color-coded on the surface, with red
and blue representing areas of negative and positive
electrostatic potential, respectively. White line, boundary of
the FAD-access cavities in both parts. Figs. 2 and 5C were
generated by using GRASP (29).
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