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PDBsum entry 2b5e
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References listed in PDB file
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Key reference
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Title
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The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites.
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Authors
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G.Tian,
S.Xiang,
R.Noiva,
W.J.Lennarz,
H.Schindelin.
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Ref.
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Cell, 2006,
124,
61-73.
[DOI no: ]
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PubMed id
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Abstract
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Protein disulfide isomerase plays a key role in catalyzing the folding of
secretory proteins. It features two catalytically inactive thioredoxin domains
inserted between two catalytically active thioredoxin domains and an acidic
C-terminal tail. The crystal structure of yeast PDI reveals that the four
thioredoxin domains are arranged in the shape of a twisted "U" with
the active sites facing each other across the long sides of the "U."
The inside surface of the "U" is enriched in hydrophobic residues,
thereby facilitating interactions with misfolded proteins. The domain
arrangement, active site location, and surface features strikingly resemble the
Escherichia coli DsbC and DsbG protein disulfide isomerases. Biochemical studies
demonstrate that all domains of PDI, including the C-terminal tail, are required
for full catalytic activity. The structure defines a framework for rationalizing
the differences between the two active sites and their respective roles in
catalyzing the formation and rearrangement of disulfide bonds.
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Figure 4.
Figure 4. Hydrophobic Surface Features of PDI
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Figure 5.
Figure 5. Active Site Features of PDI
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2006,
124,
61-73)
copyright 2006.
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