Open AccessStructure 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).