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Protein Science (2006), 15:2217-2227. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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REVIEW

The origami of thioredoxin-like folds

Jonathan L. Pan1 and James C.A. Bardwell1,2

1 Program in Cellular and Molecular Biology, University of Michigan, Ann Arbor, Michigan 48109, USA
2 Department of Molecular, Cellular & Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA

Origami is the Japanese art of folding a piece of paper into complex shapes and forms. Much like origami of paper, Nature has used conserved protein folds to engineer proteins for a particular task. An example of a protein family, which has been used by Nature numerous times, is the thioredoxin superfamily. Proteins in the thioredoxin superfamily are all structured with a beta-sheet core surrounded with {alpha}-helices, and most contain a canonical CXXC motif. The remarkable feature of these proteins is that the link between them is the fold; however, their reactivity is different for each member due to small variations in this general fold as well as their active site. This review attempts to unravel the minute differences within this protein family, and it also demonstrates the ingenuity of Nature to use a conserved fold to generate a diverse collection of proteins to perform a number of different biochemical tasks.

Keywords: thioredoxin; protein folds; glutaredoxin; glutathione S-transferase; Dsb; alkylhydroperoxidase; protein engineering


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