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PDBsum entry 3zut
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PDB id:
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Transferase
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Title:
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The structure of ost1 (d160a) kinase
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Structure:
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Serine/threonine-protein kinase srk2e. Chain: a, b. Synonym: protein open stomata 1,snf1-related kinase 2.6,snrk2.6, serine/threonine-protein kinase ost1. Engineered: yes. Mutation: yes
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Source:
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Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: srk2e, ost1, snrk2.6, at4g33950, f17i5.140. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta
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Resolution:
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2.50Å
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R-factor:
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0.200
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R-free:
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0.251
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Authors:
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C.Yunta,M.Martinez-Ripoll,A.Albert
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Key ref:
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C.Yunta
et al.
(2011).
The structure of Arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress.
J Mol Biol,
414,
135-144.
PubMed id:
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Date:
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20-Jul-11
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Release date:
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12-Oct-11
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PROCHECK
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Headers
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References
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Q940H6
(SRK2E_ARATH) -
Serine/threonine-protein kinase SRK2E from Arabidopsis thaliana
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Seq:
Struc:
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362 a.a.
281 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Mol Biol
414:135-144
(2011)
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PubMed id:
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The structure of Arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress.
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C.Yunta,
M.Martínez-Ripoll,
J.K.Zhu,
A.Albert.
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ABSTRACT
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SnRK [SNF1 (sucrose non-fermenting-1)-related protein kinase] 2.6 [open stomata
1 (OST1)] is well characterized at molecular and physiological levels to control
stomata closure in response to water-deficit stress. OST1 is a member of a
family of 10 protein kinases from Arabidopsis thaliana (SnRK2) that integrates
abscisic acid (ABA)-dependent and ABA-independent signals to coordinate the cell
response to osmotic stress. A subgroup of protein phosphatases type 2C binds
OST1 and keeps the kinase dephosphorylated and inactive. Activation of OST1
relies on the ABA-dependent inhibition of the protein phosphatases type 2C and
the subsequent self-phosphorylation of the kinase. The OST1 ABA-independent
activation depends on a short sequence motif that is conserved among all the
members of the SnRK2 family. However, little is known about the molecular
mechanism underlying this regulation. The crystallographic structure of OST1
shows that ABA-independent regulation motif stabilizes the conformation of the
kinase catalytically essential α C helix, and it provides the basis of the
ABA-independent regulation mechanism for the SnRK2 family of protein kinases.
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