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PDBsum entry 5id2
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Oxidoreductase
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PDB id
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5id2
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References listed in PDB file
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Key reference
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Title
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Redox chemistry of mycobacterium tuberculosis alkylhydroperoxide reductase e (ahpe): structural and mechanistic insight into a mycoredoxin-1 independent reductive pathway of ahpe via mycothiol.
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Authors
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A.Kumar,
A.M.Balakrishna,
W.Nartey,
M.S.Manimekalai,
G.Grüber.
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Ref.
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Free Radic Biol Med, 2016,
97,
588-601.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Secondary reference #1
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Title
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Crystal structure of ahpe from mycobacterium tuberculosis, A 1-Cys peroxiredoxin.
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Authors
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S.Li,
N.A.Peterson,
M.Y.Kim,
C.Y.Kim,
L.W.Hung,
M.Yu,
T.Lekin,
B.W.Segelke,
J.S.Lott,
E.N.Baker.
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Ref.
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J Mol Biol, 2005,
346,
1035-1046.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. Oligomerization of AhpE. (a) The AhpE dimer,
characterized by mostly hydrophobic interactions across a
non-crystallographic 2-fold axis. Prominent contributors to the
interface are the two a3 helices and the two b6-b7 hairpin
loops. Side-chains in the interface are shown in stick mode. (b)
The AhpE octamer, formed by operation of the crystallographic
4-fold axis, relating four dimers.
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Figure 5.
Figure 5. AhpE surface in the vicinity of the active site.
(a) The oxidized AhpE structure, in which Cys45 forms a sulfenic
acid, Arg116 is directed away, and a large surface channel
approaches the active site. (b) Reduced AhpE, seen in molecule B
of the bromide-soaked structure, with Arg116 directed towards
Cys45 Sg, and no surface channel except for a deep, positively
charged cavity leading to Cys45.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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