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PDBsum entry 3a2v
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Oxidoreductase
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PDB id
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3a2v
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References listed in PDB file
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Key reference
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Title
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Crystal structure of peroxiredoxin from aeropyrum pernix k1 complexed with its substrate, Hydrogen peroxide.
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Authors
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T.Nakamura,
Y.Kado,
T.Yamaguchi,
H.Matsumura,
K.Ishikawa,
T.Inoue.
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Ref.
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J Biochem (tokyo), 2010,
147,
109-115.
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PubMed id
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Abstract
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Peroxiredoxin (Prx) reduces hydrogen peroxide and alkyl peroxides to water and
corresponding alcohols, respectively. The reaction is dependent on a peroxidatic
cysteine, whose sulphur atom nucleophilically attacks one of the oxygen atoms of
the peroxide substrate. In spite of the many structural studies that have been
carried out on this reaction, the tertiary structure of the hydrogen
peroxide-bound form of Prx has not been elucidated. In this paper, we report the
crystal structure of Prx from Aeropyrum pernix K1 in the peroxide-bound form.
The conformation of the polypeptide chain is the same as that in the reduced
apo-form. The hydrogen peroxide molecule is in close contact with the
peroxidatic Cys50 and the neighbouring Thr47 and Arg126 side chain atoms, as
well as with the main chain nitrogen atoms of Val49 and Cys50. Bound peroxide
was also observed in the mutant C50S, in which the peroxidatic cysteine was
replaced by serine. Therefore, the sulphur atom of the peroxidatic cysteine is
not essential for peroxide binding, although it enhances the binding affinity.
Hydrogen peroxide binds to the protein so that it fills the active site pocket.
This study provides insight into the early stage of the Prx reaction.
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