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PDBsum entry 2zsh
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Hormone receptor
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PDB id
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2zsh
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References listed in PDB file
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Key reference
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Title
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Gibberellin-Induced della recognition by the gibberellin receptor gid1.
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Authors
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K.Murase,
Y.Hirano,
T.P.Sun,
T.Hakoshima.
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Ref.
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Nature, 2008,
456,
459-463.
[DOI no: ]
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PubMed id
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Abstract
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Gibberellins control a range of growth and developmental processes in higher
plants and have been widely used in the agricultural industry. By binding to a
nuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulate
gene expression by promoting degradation of the transcriptional regulator DELLA
proteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in which
GID1 discriminates and becomes activated by bioactive gibberellins for specific
binding to DELLA proteins remains unclear. Here we present the crystal structure
of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin and
the amino-terminal DELLA domain of GAI. In this complex, GID1A occludes
gibberellin in a deep binding pocket covered by its N-terminal helical switch
region, which in turn interacts with the DELLA domain containing DELLA, VHYNP
and LExLE motifs. Our results establish a structural model of a plant hormone
receptor that is distinct from the mechanism of the hormone perception and
effector recognition of the known auxin receptors.
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Figure 3.
Figure 3: Recognition of GA[3] by GID1A. a, A top view of the
GID1A-bound GA[3]. GID1A residues that contact GA[3] are
highlighted in yellow (the core domain) or cyan (the N-terminal
extension) and shown as stick models with van der Waals surfaces
(dots) and hydrogen bonds (dotted lines). Omit electron density
for GA[3] is shown in 3.5 contour
(red). b, A side view showing nonpolar contacts between
N-terminal extension helix b
and the GA[3] aliphatic rings. c, A top view of the hydroxyl
groups of GA[3]. d, The bound GA[3] (green) superimposes onto
GA[4] (pink) with a small root mean squared deviation (0.20
Å). Water molecules are shown as blue or red spheres.
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Figure 5.
Figure 5: Recognition of the DELLA domain by GID1A. a, A top
view of the GID1A core domain (light blue) and the N-terminal
extension (cyan) with the GAI DELLA domain (pink). The view
corresponds to Fig. 2b, d. b, A close-up view of the thumb helix
A
hooked onto the GID1A crevice. Residues of the DELLA motif
(residues D28–V38) are highlighted in green. Hydrogen bonds
are indicated with dotted lines. A bridging water molecule
inside the loop is shown as a red sphere. c, The LExLE motif
(M43–M57). d, The VHYNP motif (T72–M87). In b–d, the
residues in each motif that directly contact GID1A are
highlighted in green.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2008,
456,
459-463)
copyright 2008.
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