Ontology highlight
ABSTRACT:
SUBMITTER: Mu Y
PROVIDER: S-EPMC3581551 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Mu Yinnan Y Lian Fu-Ming FM Teng Yan-Bin YB Ao Jingqun J Jiang Yong-Liang YL He Yong-Xing YX Chen Yuxing Y Zhou Cong-Zhao CZ Chen Xinhua X
PloS one 20130225 2
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 pe ...[more]