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PDBsum entry 3ed1
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Hydrolase receptor
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PDB id
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3ed1
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase receptor
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Title:
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Crystal structure of rice gid1 complexed with ga3
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Structure:
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Gibberellin receptor gid1. Chain: a, b, c, d, e, f. Synonym: gibberellin-insensitive dwarf protein 1, protein gibberellin insensitive dwarf1. Engineered: yes
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Source:
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Oryza sativa subsp. Japonica. Rice. Organism_taxid: 39947. Gene: gid1, os05g0407500, loc_os05g33730, oj1657_h11.10, p0040b10.6. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.90Å
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R-factor:
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0.199
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R-free:
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0.239
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Authors:
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A.Shimada,T.Nakatsu,M.Ueguchi-Tanaka,H.Kato,M.Matsuoka
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Key ref:
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A.Shimada
et al.
(2008).
Structural basis for gibberellin recognition by its receptor GID1.
Nature,
456,
520-523.
PubMed id:
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Date:
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02-Sep-08
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Release date:
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25-Nov-08
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PROCHECK
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Headers
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References
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Nature
456:520-523
(2008)
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PubMed id:
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Structural basis for gibberellin recognition by its receptor GID1.
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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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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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L.B.Sheard,
X.Tan,
H.Mao,
J.Withers,
G.Ben-Nissan,
T.R.Hinds,
Y.Kobayashi,
F.F.Hsu,
M.Sharon,
J.Browse,
S.Y.He,
J.Rizo,
G.A.Howe,
and
N.Zheng
(2010).
Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-receptor.
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Nature,
468,
400-405.
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PDB codes:
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A.Santner,
and
M.Estelle
(2009).
Recent advances and emerging trends in plant hormone signalling.
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Nature,
459,
1071-1078.
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N.Nishimura,
K.Hitomi,
A.S.Arvai,
R.P.Rambo,
C.Hitomi,
S.R.Cutler,
J.I.Schroeder,
and
E.D.Getzoff
(2009).
Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.
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Science,
326,
1373-1379.
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PDB code:
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R.D.Vierstra
(2009).
The ubiquitin-26S proteasome system at the nexus of plant biology.
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Nat Rev Mol Cell Biol,
10,
385-397.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
