Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii.

Abstract

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).

DOI: 10.1107/S1744309113014036

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@article{Nakamura2013StructureOP, title={Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii.}, author={Tsutomu Nakamura and Aika Mori and Mayumi Niiyama and Hiroyoshi Matsumura and Chisa Tokuyama and Junji Morita and Koichi Uegaki and Tsuyoshi Inoue}, journal={Acta crystallographica. Section F, Structural biology and crystallization communications}, year={2013}, volume={69 Pt 7}, pages={719-22} }