2OE1

Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae (reduced form)

Summary for 2OE1

• Entry DOI: 10.2210/pdb2oe1/pdb
• Related: 2OE0 2OE3
• Descriptor: Thioredoxin-3, SULFATE ION (3 entities in total)
• Functional Keywords: electron transport, alpha/beta sandwich, reduced, dimer
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Mitochondrion: P25372
• Total number of polymer chains: 2
• Total formula weight: 26026.06

Authors

Bao, R.,Zhang, Y.R.,Zhou, C.Z.,Chen, Y.X. (deposition date: 2006-12-28, release date: 2008-01-08, Last modification date: 2023-10-25)

Primary citation

Bao, R.,Zhang, Y.R.,Zhou, C.-Z.,Chen, Y.X.
Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues
Biochim.Biophys.Acta, 1794:716-721, 2009

PubMed Abstract: 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 A, 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.

PubMed: 19166985
DOI: 10.1016/j.bbapap.2008.12.016

Experimental method

X-RAY DIFFRACTION (2.1 Å)