title: Crystal structures of human peroxiredoxin 6 in different oxidation states.
abstract: Peroxiredoxins (Prxs) are a family of antioxidant enzymes found ubiquitously. Prxs function not only as H2O2 scavengers but also as highly sensitive H2O2 sensors and signal transducers. Since reactive oxygen species are involved in many cellular metabolic and signaling processes, Prxs play important roles in various diseases. Prxs can be hyperoxidized to the sulfinic acid (SO2H) or sulfonic acid (SO3H) forms in the presence of high concentrations of H2O2. It is known that oligomerization of Prx is changed accompanying oxidation states, and linked to the function. Among the six Prxs in mammals, Prx6 is the only 1-Cys Prx. It is found in all organs in humans, unlike some 2-Cys Prxs, and is present in all species from bacteria to humans. In addition, Prx6 has Ca(2+)-independent phospholipase A2 (PLA2) activity. Thus far only the crystal structure of Prx in the oxidized state has been reported. In this study, we present the crystal structures of human Prx6 in the reduced (SH) and the sulfinic acid (SO2H) forms.
authors.affiliation: Biomedical Research Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea; Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea.
authors.forename: Kyung Hee
authors.initials: KH
authors.lastname: Kim
authors.affiliation: Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea. Electronic address: wlee@spin.yonsei.ac.kr.
authors.forename: Weontae
authors.initials: W
authors.lastname: Lee
authors.affiliation: Biomedical Research Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea. Electronic address: eunice@kist.re.kr.
authors.forename: Eunice EunKyeong
authors.initials: EE
authors.lastname: Kim
mesh_terms: D001665:Binding Sites; D003545:Cysteine / Q000737:chemistry*; D019281:Dimerization; D004789:Enzyme Activation; D006801:Humans; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry*; D054465:Peroxiredoxin VI / Q000737:chemistry* / Q000648:ultrastructure*; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: C515977:PRDX6 protein, human; D054465:Peroxiredoxin VI; D003545:Cysteine; D010100:Oxygen
keywords: 1-Cys Prx; Active site; Crystal structure; Oxidation; Prx6; Reduction