Crystal structure of the C47S mutant of human peroxiredoxin 5
(2004) Journal of Chemical Crystallography — Vol. 34, n° 8, p. 553-558 (2004)
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- Abstract
- In the crystal structure of the reduced form of the wild-type human peroxiredoxin 5, the presence of a benzoate ion in direct interaction with the peroxidatic cysteine (Cys 47) appeared as a rather intriguing feature since it is known that the benzoate ion can play the role of a specific hydroxyl radical scavenger. The crystal structure of the C47S mutant of the same enzyme has been crystallized in the tetragonal system, space group P4(1)2(1)2, with a = 65.65 Angstrom, c = 122.04 Angstrom. It confirms the presence of this benzoate ion in spite of the mutation into a serine of the Cys 47 residue to which the benzoate ion was directly linked in the wild-type structure. The benzoate ion seems to be stabilized by hydrophobic contacts on both sides of the aromatic ring. In this matter, the alpha5 helix, which is specific to peroxiredoxin 5 among mammalian peroxiredoxins, plays an important role. These hydrophobic contacts also allow to suggest why the benzoate ion disappears when the molecule is oxidized.
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Evrard, C.-M., Declercq, J.-P., Smeets, A., & Knoops, B. (2004). Crystal structure of the C47S mutant of human peroxiredoxin 5. Journal of Chemical Crystallography, 34(8), 553-558. https://doi.org/10.1023/B:JOCC.0000042025.08082.6c (Original work published 2004)