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PDBsum entry 2zuq
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Oxidoreductase/immune system
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PDB id
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2zuq
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Contents |
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148 a.a.
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218 a.a.
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216 a.a.
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* Residue conservation analysis
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PDB id:
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Oxidoreductase/immune system
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Title:
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Crystal structure of dsbb-fab complex
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Structure:
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Disulfide bond formation protein b. Chain: a, d. Synonym: dsbb, disulfide oxidoreductase. Engineered: yes. Mutation: yes. Fab fragment light chain. Chain: b, e. Fab fragment heavy chain. Chain: c, f
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Source:
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Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: dsbb. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090.
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Resolution:
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3.30Å
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R-factor:
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0.279
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R-free:
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0.351
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Authors:
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K.Inaba,M.Suzuki,S.Murakami
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Key ref:
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K.Inaba
et al.
(2009).
Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB.
Embo J,
28,
779-791.
PubMed id:
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Date:
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28-Oct-08
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Release date:
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14-Apr-09
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PROCHECK
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Headers
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References
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P0A6M2
(DSBB_ECOLI) -
Disulfide bond formation protein B from Escherichia coli (strain K12)
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Seq:
Struc:
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176 a.a.
148 a.a.*
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Embo J
28:779-791
(2009)
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PubMed id:
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Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB.
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K.Inaba,
S.Murakami,
A.Nakagawa,
H.Iida,
M.Kinjo,
K.Ito,
M.Suzuki.
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ABSTRACT
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In the Escherichia coli system catalysing oxidative protein folding, disulphide
bonds are generated by the cooperation of DsbB and ubiquinone and transferred to
substrate proteins through DsbA. The structures solved so far for different
forms of DsbB lack the Cys104-Cys130 initial-state disulphide that is directly
donated to DsbA. Here, we report the 3.4 A crystal structure of a DsbB-Fab
complex, in which DsbB has this principal disulphide. Its comparison with the
updated structure of the DsbB-DsbA complex as well as with the recently reported
NMR structure of a DsbB variant having the rearranged Cys41-Cys130 disulphide
illuminated conformational transitions of DsbB induced by the binding and
release of DsbA. Mutational studies revealed that the membrane-parallel short
alpha-helix of DsbB has a key function in physiological electron flow,
presumably by controlling the positioning of the Cys130-containing loop. These
findings demonstrate that DsbB has developed the elaborate conformational
dynamism to oxidize DsbA for continuous protein disulphide bond formation in the
cell.
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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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S.Hwang,
and
C.Hilty
(2011).
Folding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopy.
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Proteins,
79,
1365-1375.
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PDB codes:
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S.R.Shouldice,
B.Heras,
P.M.Walden,
M.Totsika,
M.A.Schembri,
and
J.L.Martin
(2011).
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
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Antioxid Redox Signal,
14,
1729-1760.
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A.M.Lasica,
A.Wyszynska,
K.Szymanek,
P.Majewski,
and
E.K.Jagusztyn-Krynicka
(2010).
Campylobacter protein oxidation influences epithelial cell invasion or intracellular survival as well as intestinal tract colonization in chickens.
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J Appl Genet,
51,
383-393.
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G.Malojcić,
and
R.Glockshuber
(2010).
The PAPS-independent aryl sulfotransferase and the alternative disulfide bond formation system in pathogenic bacteria.
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Antioxid Redox Signal,
13,
1247-1259.
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H.Kadokura,
and
J.Beckwith
(2010).
Mechanisms of oxidative protein folding in the bacterial cell envelope.
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Antioxid Redox Signal,
13,
1231-1246.
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J.A.Lundbaek,
S.A.Collingwood,
H.I.Ingólfsson,
R.Kapoor,
and
O.S.Andersen
(2010).
Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes.
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J R Soc Interface,
7,
373-395.
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K.Inaba
(2010).
Structural basis of protein disulfide bond generation in the cell.
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Genes Cells,
15,
935-943.
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K.R.Vinothkumar,
and
R.Henderson
(2010).
Structures of membrane proteins.
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Q Rev Biophys,
43,
65.
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W.Li,
S.Schulman,
R.J.Dutton,
D.Boyd,
J.Beckwith,
and
T.A.Rapoport
(2010).
Structure of a bacterial homologue of vitamin K epoxide reductase.
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Nature,
463,
507-512.
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PDB codes:
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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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