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PDBsum entry 3ebl
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Hydrolase receptor
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PDB id
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3ebl
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References listed in PDB file
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Key reference
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Title
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Structural basis for gibberellin recognition by its receptor gid1.
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Authors
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A.Shimada,
M.Ueguchi-Tanaka,
T.Nakatsu,
M.Nakajima,
Y.Naoe,
H.Ohmiya,
H.Kato,
M.Matsuoka.
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Ref.
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Nature, 2008,
456,
520-523.
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PubMed id
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Abstract
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Gibberellins (GAs) are phytohormones essential for many developmental processes
in plants. A nuclear GA receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), has a
primary structure similar to that of the hormone-sensitive lipases (HSLs). Here
we analyse the crystal structure of Oryza sativa GID1 (OsGID1) bound with GA(4)
and GA(3) at 1.9 A resolution. The overall structure of both complexes shows an
alpha/beta-hydrolase fold similar to that of HSLs except for an amino-terminal
lid. The GA-binding pocket corresponds to the substrate-binding site of HSLs. On
the basis of the OsGID1 structure, we mutagenized important residues for GA
binding and examined their binding activities. Almost all of them showed very
little or no activity, confirming that the residues revealed by structural
analysis are important for GA binding. The replacement of Ile 133 with Leu or
Val-residues corresponding to those of the lycophyte Selaginella moellendorffii
GID1s-caused an increase in the binding affinity for GA(34), a
2beta-hydroxylated GA(4). These observations indicate that GID1 originated from
HSL and was further modified to have higher affinity and more strict selectivity
for bioactive GAs by adapting the amino acids involved in GA binding in the
course of plant evolution.
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