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PDBsum entry 3dd9
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Ribosome inhibitor
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PDB id
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3dd9
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Contents |
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117 a.a.
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122 a.a.
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110 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Ribosome inhibitor
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Title:
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Structure of doch66y dimer
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Structure:
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Death on curing protein. Chain: a, b, c, d, e, f, g, h. Engineered: yes. Mutation: yes
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Source:
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Enterobacteria phage p1. Organism_taxid: 10678. Gene: doc. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.45Å
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R-factor:
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0.213
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R-free:
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0.245
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Authors:
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A.Garcia-Pino,R.Loris
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Key ref:
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S.De Gieter
et al.
(2014).
The intrinsically disordered domain of the antitoxin Phd chaperones the toxin Doc against irreversible inactivation and misfolding.
J Biol Chem,
289,
34013-34023.
PubMed id:
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Date:
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05-Jun-08
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Release date:
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09-Jun-09
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PROCHECK
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Headers
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References
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Q06259
(DOC_BPP1) -
Protein kinase doc from Escherichia phage P1
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Seq:
Struc:
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126 a.a.
117 a.a.*
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Enzyme class:
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Chains A, B, C, D, E, F, G, H:
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 Biol Chem
289:34013-34023
(2014)
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PubMed id:
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The intrinsically disordered domain of the antitoxin Phd chaperones the toxin Doc against irreversible inactivation and misfolding.
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S.De Gieter,
A.Konijnenberg,
A.Talavera,
A.Butterer,
S.Haesaerts,
H.De Greve,
F.Sobott,
R.Loris,
A.Garcia-Pino.
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ABSTRACT
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The toxin Doc from the phd/doc toxin-antitoxin module targets the cellular
translation machinery and is inhibited by its antitoxin partner Phd. Here we
show that Phd also functions as a chaperone, keeping Doc in an active, correctly
folded conformation. In the absence of Phd, Doc exists in a relatively expanded
state that is prone to dimerization through domain swapping with its active site
loop acting as hinge region. The domain-swapped dimer is not capable of
arresting protein synthesis in vitro, whereas the Doc monomer is. Upon binding
to Phd, Doc becomes more compact and is secured in its monomeric state with a
neutralized active site.
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Links
