Multiple catalytically active thioredoxin folds: a winning strategy for many functions.
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).
Pedone
Emilia
E
Istituto di Biostrutture e Bioimmagini-CNR, Naples, Italy.
Limauro
Danila
D
D'Ambrosio
Katia
K
De Simone
Giuseppina
G
Bartolucci
Simonetta
S
D000595:Amino Acid Sequence; D000818:Animals; D001105:Archaea / Q000737:chemistry / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D001419:Bacteria / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D020134:Catalytic Domain; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D054464:Peroxiredoxins / Q000737:chemistry* / Q000378:metabolism; D019704:Protein Disulfide-Isomerases / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D013879:Thioredoxins; D010088:Oxidoreductases; D054464:Peroxiredoxins; D019704:Protein Disulfide-Isomerases