title: The N-terminal β-sheet of peroxiredoxin 4 in the large yellow croaker Pseudosciaena crocea is involved in its biological functions.
abstract: Peroxiredoxins (Prxs) are thiol-specific antioxidant proteins that exhibit peroxidase and peroxynitrite reductase activities involved in the reduction of reactive oxygen species. The peroxiredoxin Prx4 from the large yellow croaker Pseudosciaena crocea is a typical 2-Cys Prx with an N-terminal signal peptide. We solved the crystal structure of Prx4 at 1.90 Å and revealed an N-terminal antiparallel β-sheet that contributes to the dimer interface. Deletion of this β-sheet decreased the in vitro peroxidase activity to about 50% of the wild-type. In vivo assays further demonstrated that removal of this β-sheet led to some impairment in the ability of Prx4 to negatively regulate nuclear factor-κB (NF-κB) activity and to perform its role in anti-bacterial immunity. These results provide new insights into the structure and function relationship of a peroxiredoxin from bony fish.
authors: Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen, Fujian, People's Republic of China.
authors: Yinnan
authors: Y
authors: Mu
authors: Fu-Ming
authors: FM
authors: Lian
authors: Yan-Bin
authors: YB
authors: Teng
authors: Jingqun
authors: J
authors: Ao
authors: Yong-Liang
authors: YL
authors: Jiang
authors: Yong-Xing
authors: YX
authors: He
authors: Yuxing
authors: Y
authors: Chen
authors: Cong-Zhao
authors: CZ
authors: Zhou
authors: Xinhua
authors: X
authors: Chen
mesh_terms: D000818:Animals; D019281:Dimerization; D016328:NF-kappa B / Q000378:metabolism; D010473:Perciformes; D054464:Peroxiredoxins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation; D017384:Sequence Deletion
chemical_list: D016328:NF-kappa B; D054464:Peroxiredoxins