Thioredoxins are small, heat-stable proteins, present in all living organisms. They are involved in a large number of cellular processes,1 functioning as disulfide oxido-reduc- tases through the reversible oxidation of their cysteine resi- dues present in a conserved active site. The yeast Sacharo- myces cerevisiae contains three different isoforms of thiore- doxin: Trx1 and Trx2 are cytoplasmic2 and Trx3 is mitochondrial.3 Yeast cytoplasmic thioredoxins share 78% identity in primary sequence [Fig. 1(A)]. Trx2 appears to play the predominant role against oxidative stress since its expression increases in response to hydroperoxides, whereas Trx1 expression remains unaffected.4 Despite the amount of knowledge concerning the conserved Trx folding, struc- tural details need to be better elucidated to understand thi- oredoxin ability to interact with multiple cellular targets. In the present work, we report the first high-resolution structure of Trx1 from Sacharomyces cerevisiae and discuss the structural features that are possibly related to the bind- ing and specificity with diverse cellular targets.
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