3F3R

Crystal structure of yeast Thioredoxin1-glutathione mixed disulfide complex

Summary for 3F3R

• Entry DOI: 10.2210/pdb3f3r/pdb
• Related: 3F3Q
• Descriptor: Thioredoxin-1, GLUTATHIONE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: electron transport, thioredoxin, glutathione, deoxyribonucleotide synthesis, golgi apparatus, membrane, nucleus, protein transport, redox-active center, phosphoprotein, transport
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm: P22217
• Total number of polymer chains: 2
• Total formula weight: 25018.33

Authors

Zhang, Y.R.,Bao, R.,Zhou, C.Z.,Chen, Y.X. (deposition date: 2008-10-31, release date: 2009-10-20, Last modification date: 2023-11-01)

Primary citation

Bao, R.,Zhang, Y.R.,Lou, X.,Zhou, C.Z.,Chen, Y.X.
Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: implications for the catalytic mechanism of GSSG reduced by the thioredoxin system
Biochim.Biophys.Acta, 1794:1218-1223, 2009

PubMed Abstract: Thioredoxin (Trx) and glutathione/glutaredoxin (GSH/Grx) systems play the dominant role in cellular redox homeostasis. Recently the Trx system has been shown to be responsible to control the balance of GSH/GSSG once the glutathione reductase system is not available. To decipher the structural basis of electron transfer from the Trx system to GSSG, we solved the crystal structures of oxidized Trx1 and glutathionylated Trx1Cys33Ser mutant at 1.76 and 1.80 A, respectively. Comparative structural analysis revealed a key residue Met35 involved in the Trx-GSSG recognition. Subsequent mutagenesis and kinetic studies proved that Met35Arg mutation could alter the apparent K(m) and V(max) values of the reaction. These findings gave us the structural insights into GSSG reduction catalyzed by the Trx system.

PubMed: 19362171
DOI: 10.1016/j.bbapap.2009.04.001

Experimental method

X-RAY DIFFRACTION (1.8 Å)