1PRX

HORF6 A NOVEL HUMAN PEROXIDASE ENZYME

Summary for 1PRX

• Entry DOI: 10.2210/pdb1prx/pdb
• Descriptor: HORF6 (2 entities in total)
• Functional Keywords: peroxiredoxin, horf6, hydrogen peroxide, redox regulation, cellular signaling, antioxidant
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P30041
• Total number of polymer chains: 2
• Total formula weight: 50135.81

Authors

Choi, H.-J.,Kang, S.W.,Yang, C.-H.,Rhee, S.G.,Ryu, S.-E. (deposition date: 1998-04-03, release date: 1998-06-17, Last modification date: 2024-10-30)

Primary citation

Choi, H.J.,Kang, S.W.,Yang, C.H.,Rhee, S.G.,Ryu, S.E.
Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
Nat.Struct.Biol., 5:400-406, 1998

PubMed Abstract: Hydrogen peroxide (H2O2) has been implicated recently as an intracellular messenger that affects cellular processes including protein phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor. The crystal structure of a human Prx enzyme, hORF6, reveals that the protein contains two discrete domains and forms a dimer. The N-terminal domain has a thioredoxin fold and the C-terminal domain is used for dimerization. The active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket. The positively charged environment surrounding Cys 47 accounts for the peroxidase activity of the enzyme, which contains no redox cofactors.

PubMed: 9587003
DOI: 10.1038/nsb0598-400

Experimental method

X-RAY DIFFRACTION (2 Å)