期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1794, 期 4, 页码 716-721出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2008.12.016
关键词
Thioredoxin; Saccharomyces cerevisiae; Crystal structure; Mitochondrion; S-nitrosylation
资金
- Ministry of Science and Technology of China [2006CB910202, 2006CB806501]
- Ministry of Education of China [NCET-06-0374, PRA B07-02]
- National Natural Science Foundation of China [30670461, 30470366]
- Chinese Academy of Science
- USTC
The yeast Saccharomyces cerevisiae Trx3 is a key member of the thioredoxin system to control the cellular redox homeostasis in mitochondria. We solved the crystal structures of yeast Trx3 in oxidized and reduced forms at 1.80 and 2.10 angstrom, respectively. Besides the active site, the additional cysteine residue Cys69 also undergoes a significant redox-correlated conformational change. Comparative structural analyses in combination with activity assays revealed that residue Cys69 could be S-nitrosylated in vitro. S-nitrosylation of Cys69 will decrease the activity of Trx3 by 20%, which is comparable to the effect of the Cys69Ser mutation. Taken together, these findings provided us some new insights into the putative function of the additional cysteine residues of Trx3. (C) 2009 Elsevier B.V. All rights reserved.
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