Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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 α-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.
Originalsprog | Engelsk |
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Tidsskrift | Structure |
Vol/bind | 14 |
Udgave nummer | 11 |
Sider (fra-til) | 1701-1710 |
Antal sider | 10 |
ISSN | 0969-2126 |
DOI | |
Status | Udgivet - 2006 |
Eksternt udgivet | Ja |
ID: 240161387