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PDBsum entry 4rj9
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PDB id:
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Ligase
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Title:
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Structure of a plant specific c2 domain protein, osgap1 from rice
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Structure:
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C2 domain-containing protein-like. Chain: a. Synonym: g-protein binding protein, os02g0327000 protein, cdna clone:006-212-c07, full insert sequence, cdna clone:j033052d22, full insert sequence. Engineered: yes
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Source:
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Oryza sativa japonica group. Japonica rice. Organism_taxid: 39947. Gene: os02g0327000, osgap1, osjnbb0042g06.10, osj_06508, p0476c12.36. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.63Å
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R-factor:
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0.185
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R-free:
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0.204
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Authors:
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R.Miao,Y.H.Fong,K.B.Wong,H.M.Lam
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Key ref:
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Y.L.Yung
et al.
(2015).
Site-directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 for the Physiological Functions of the Rice GTPase-activating Protein 1 (OsGAP1).
J Biol Chem,
290,
23984-23996.
PubMed id:
DOI:
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Date:
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08-Oct-14
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Release date:
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26-Aug-15
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PROCHECK
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Headers
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References
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Q6YWF1
(GAP1_ORYSJ) -
GTPase activating protein 1 from Oryza sativa subsp. japonica
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Seq:
Struc:
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165 a.a.
161 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.6.5.1.1
- Dna ligase (ATP).
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Reaction:
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ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate
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ATP
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+
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(deoxyribonucleotide)n-3'-hydroxyl
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+
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5'-phospho- (deoxyribonucleotide)m
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=
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(deoxyribonucleotide)n+m
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+
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AMP
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+
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Biol Chem
290:23984-23996
(2015)
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PubMed id:
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Site-directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 for the Physiological Functions of the Rice GTPase-activating Protein 1 (OsGAP1).
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Y.L.Yung,
M.Y.Cheung,
R.Miao,
Y.H.Fong,
K.P.Li,
M.H.Yu,
M.L.Chye,
K.B.Wong,
H.M.Lam.
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ABSTRACT
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The C2 domain is one of the most diverse phospholipid-binding domains mediating
cellular signaling. One group of C2-domain proteins are plant-specific and are
characterized by their small sizes and simple structures. We have previously
reported that a member of this group, OsGAP1, is able to alleviate salt stress
and stimulate defense responses, and bind to both phospholipids and an
unconventional G-protein, OsYchF1. Here we solved the crystal structure of
OsGAP1 to a resolution of 1.63 Å. Using site-directed mutagenesis, we
successfully differentiated between the clusters of surface residues that are
required for binding to phospholipids versus OsYchF1, which, in turn, is
critical for its role in stimulating defense responses. On the other hand, the
ability to alleviate salt stress by OsGAP1 is dependent only on its ability to
bind OsYchF1 and is independent of its phospholipid-binding activity.
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Links
