Abstract
The Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded β-sheet surrounded by three α-helices. Various insertions are possible on this structural theme originating different proteins, which show a variety of functions and specificities. During evolution, the assembly of different Trx fold domains has been used many times to build new multi-domain proteins able to perform a large number of catalytic functions. To clarify the interaction mode of the different Trx domains within a multi-domain structure and how their combination can affect catalytic performances, in this review, we report on a structural and functional analysis of the most representative proteins containing more than one catalytically active Trx domain: the eukaryotic protein disulfide isomerases (PDIs), the thermophilic protein disulfide oxidoreductases (PDOs) and the hybrid peroxiredoxins (Prxs).
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Pedone, E., Limauro, D., D’Ambrosio, K. et al. Multiple catalytically active thioredoxin folds: a winning strategy for many functions. Cell. Mol. Life Sci. 67, 3797–3814 (2010). https://doi.org/10.1007/s00018-010-0449-9
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DOI: https://doi.org/10.1007/s00018-010-0449-9