2IWT

Thioredoxin h2 (HvTrxh2) in a mixed disulfide complex with the target protein BASI

Summary for 2IWT

• Entry DOI: 10.2210/pdb2iwt/pdb
• Related: 1AVA
• Descriptor: THIOREDOXIN H ISOFORM 2, ALPHA-AMYLASE/SUBTILISIN INHIBITOR, CITRATE ANION, ... (4 entities in total)
• Functional Keywords: protease inhibitor, disulfide reductase, basi, amy2, redox, thioredoxin, oxidoreductase, substrate recognition, disulfide intermediate, alpha-amylase inhibitor, serine protease inhibitor
• Biological source: HORDEUM VULGARE (BARLEY); More
• Total number of polymer chains: 2
• Total formula weight: 34747.14

Authors

Maeda, K.,Hagglund, P.,Finnie, C.,Svensson, B.,Henriksen, A. (deposition date: 2006-07-04, release date: 2006-11-15, Last modification date: 2024-10-16)

Primary citation

Maeda, K.,Hagglund, P.,Finnie, C.,Svensson, B.,Henriksen, A.
Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin.
Structure, 14:1701-, 2006

PubMed 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.

PubMed: 17098195
DOI: 10.1016/J.STR.2006.09.012

Experimental method

X-RAY DIFFRACTION (2.3 Å)