Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon  Pyrococcus horikoshii | Zendy

Nakamura Tsutomu | Zendy; Mori Aika | Zendy; Niiyama Mayumi | Zendy; Matsumura Hiroyoshi | Zendy; Tokuyama Chisa | Zendy; Morita Junji | Zendy; Uegaki Koichi | Zendy; Inoue Tsuyoshi | Zendy

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Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii

Author(s) -

Nakamura Tsutomu,

Mori Aika,

Niiyama Mayumi,

Matsumura Hiroyoshi,

Tokuyama Chisa,

Morita Junji,

Uegaki Koichi,

Inoue Tsuyoshi

Publication year - 2013

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309113014036

Subject(s) - pyrococcus horikoshii , peroxiredoxin , chemistry , residue (chemistry) , crystallography , crystallization , cysteine , biochemistry , stereochemistry , crystal structure , enzyme , organic chemistry , peroxidase

The crystal structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii (PhPrx) was determined at a resolution of 2.25 Å. The overall structure was a ring‐type decamer consisting of five homodimers. Citrate, which was included in the crystallization conditions, was bound to the peroxidatic cysteine of the active site, with two O atoms of the carboxyl group mimicking those of the substrate hydrogen peroxide. PhPrx lacked the C‐terminal tail that forms a 32‐residue extension of the protein in the homologous peroxiredoxin from Aeropyrum pernix (ApPrx).

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