1. Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeonPyrococcus horikoshii
- Author
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Mayumi Niiyama, Aika Mori, Junji Morita, Koichi Uegaki, Hiroyoshi Matsumura, Tsuyoshi Inoue, Chisa Tokuyama, and Tsutomu Nakamura
- Subjects
Models, Molecular ,Protein Conformation ,Aeropyrum ,Molecular Sequence Data ,Biophysics ,Biology ,Crystallography, X-Ray ,Biochemistry ,Citric Acid ,Pyrococcus horikoshii ,Protein structure ,Structural Biology ,Genetics ,Structural Communications ,Aeropyrum pernix ,Amino Acid Sequence ,Cysteine ,Peptide sequence ,Binding Sites ,Sequence Homology, Amino Acid ,Active site ,Hydrogen Peroxide ,Peroxiredoxins ,respiratory system ,Oxidants ,Condensed Matter Physics ,biology.organism_classification ,Archaea ,Crystallography ,biology.protein ,Crystallization ,Peroxiredoxin - 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).
- Published
- 2013