Multiple catalytically active thioredoxin folds: a winning strategy for many functions |
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Authors: | Emilia Pedone Danila Limauro Katia D’Ambrosio Giuseppina De Simone Simonetta Bartolucci |
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Institution: | 1.Istituto di Biostrutture e Bioimmagini-CNR,Naples,Italy;2.Dipartimento di Biologia Strutturale e Funzionale,Università degli Studi di Napoli “Federico II”, Complesso Universitario Monte S. Angelo,Naples,Italy |
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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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Keywords: | |
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