Structural basis for target protein recognition by the protein disulfide reductase thioredoxin

Kenji Maeda, Per Hägglund, Christine Finnie, Birte Svensson, A. Henriksen

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley alpha-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides.
    Original languageEnglish
    JournalStructure
    Volume14
    Issue number11
    Pages (from-to)1701-1710
    ISSN0969-2126
    DOIs
    Publication statusPublished - 2006

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