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PDBsum entry 4ml6
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PDB id:
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Isomerase
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Title:
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Disulfide isomerase from multidrug resistance inca/c conjugative plasmid in reduced state
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Structure:
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Dsbp. Chain: a, b, c, d. Fragment: unp residues 22-235. Synonym: dsbp thiol:disulfide interchange protein, plasmid or integrative and conjugative elements encoded disulfide isomerase. Engineered: yes
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Source:
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Klebsiella pneumoniae. Organism_taxid: 573. Gene: dsbc, dsbp, pndm10469_89. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.30Å
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R-factor:
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0.193
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R-free:
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0.244
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Authors:
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L.Premkumar,F.Kurth,S.Neyer,J.L.Martin
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Key ref:
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L.Premkumar
et al.
(2014).
The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase.
J Biol Chem,
289,
2563-2576.
PubMed id:
DOI:
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Date:
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06-Sep-13
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Release date:
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11-Dec-13
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PROCHECK
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Headers
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References
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A6GV51
(A6GV51_KLEPN) -
Thiol:disulfide interchange protein from Klebsiella pneumoniae
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Seq:
Struc:
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235 a.a.
202 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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Enzyme class:
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E.C.5.3.4.1
- protein disulfide-isomerase.
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Reaction:
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Rearrangement of both intrachain and interchain disulfide bonds in proteins to form the native structures.
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DOI no:
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J Biol Chem
289:2563-2576
(2014)
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PubMed id:
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The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase.
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L.Premkumar,
F.Kurth,
S.Neyer,
M.A.Schembri,
J.L.Martin.
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ABSTRACT
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The multidrug resistance-encoding IncA/C conjugative plasmids disseminate
antibiotic resistance genes among clinically relevant enteric bacteria. A
plasmid-encoded disulfide isomerase is associated with conjugation. Sequence
analysis of several IncA/C plasmids and IncA/C-related integrative and
conjugative elements (ICE) from commensal and pathogenic bacteria identified a
conserved DsbC/DsbG homolog (DsbP). The crystal structure of DsbP reveals an
N-terminal domain, a linker region, and a C-terminal catalytic domain. A DsbP
homodimer is formed through domain swapping of two DsbP N-terminal domains. The
catalytic domain incorporates a thioredoxin-fold with characteristic CXXC and
cis-Pro motifs. Overall, the structure and redox properties of DsbP diverge from
the Escherichia coli DsbC and DsbG disulfide isomerases. Specifically, the
V-shaped dimer of DsbP is inverted compared with EcDsbC and EcDsbG. In addition,
the redox potential of DsbP (-161 mV) is more reducing than EcDsbC (-130 mV) and
EcDsbG (-126 mV). Other catalytic properties of DsbP more closely resemble those
of EcDsbG than EcDsbC. These catalytic differences are in part a consequence of
the unusual active site motif of DsbP (CAVC); substitution to the EcDsbC-like
(CGYC) motif converts the catalytic properties to those of EcDsbC. Structural
comparison of the 12 independent subunit structures of DsbP that we determined
revealed that conformational changes in the linker region contribute to mobility
of the catalytic domain, providing mechanistic insight into DsbP function. In
summary, our data reveal that the conserved plasmid-encoded DsbP protein is a
bona fide disulfide isomerase and suggest that a dedicated oxidative folding
enzyme is important for conjugative plasmid transfer.
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