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PDBsum entry 3cmi
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Oxidoreductase
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PDB id
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3cmi
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Crystal structure of glutathione-dependent phospholipid peroxidase hyr1 from the yeast saccharomyces cerevisiae
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Structure:
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Peroxiredoxin hyr1. Chain: a. Synonym: hydrogen peroxide resistance protein 1, oxidant receptor peroxidase 1, glutathione peroxidase 3, phospholipid hydroperoxide glutathione peroxidase 3, phgpx3. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: s228c. Gene: hyr1, gpx3, orp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.02Å
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R-factor:
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0.226
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R-free:
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0.256
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Authors:
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W.J.Z.Zhang,Y.X.He,J.Yu,C.Z.Zhou
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Key ref:
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W.J.Zhang
et al.
(2008).
Crystal structure of glutathione-dependent phospholipid peroxidase Hyr1 from the yeast Saccharomyces cerevisiae.
Proteins,
73,
1058-1062.
PubMed id:
DOI:
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Date:
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21-Mar-08
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Release date:
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16-Sep-08
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PROCHECK
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Headers
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References
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P40581
(GPX3_YEAST) -
Glutathione peroxidase-like peroxiredoxin HYR1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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163 a.a.
143 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.1.11.1.24
- thioredoxin-dependent peroxiredoxin.
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Reaction:
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a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]- disulfide + H2O
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hydroperoxide
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+
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[thioredoxin]-dithiol
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=
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alcohol
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+
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[thioredoxin]- disulfide
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+
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H2O
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proteins
73:1058-1062
(2008)
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PubMed id:
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Crystal structure of glutathione-dependent phospholipid peroxidase Hyr1 from the yeast Saccharomyces cerevisiae.
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W.J.Zhang,
Y.X.He,
Z.Yang,
J.Yu,
Y.Chen,
C.Z.Zhou.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. A: Cartoon representation of the overall fold of
Hyr1, colored and labeled according to the secondary structures.
Cys36 thiol was highlighted as sticks and the interrupted points
were colored with purple and connected with a gray dashed line.
B, C: Superposition of Hyr1 (red) upon rPtGpx5 (cyan) and
oPtGpx5 (gray), respectively. The helix  2
of rPtGpx5 and peroxidatic and resolving cysteine of all
structures were labeled. D: Hyr1 peroxidase activity assays.
Assays were performed separately for three times in the presence
of Trx2, Trr1, NADPH, and H[2]O[2], with Hyr1 (filled squares),
with Hyr1-Cys82Ser mutant (open triangles), without Hyr1 as a
null control (filled circles). Data are expressed as the
decrement of OD[340 nm] against time in minute. The error bars
represent the standard deviations.
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The above figure is
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
73,
1058-1062)
copyright 2008.
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Links
