2iwt
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Thioredoxin is ubiquitous and regulates various target proteins through | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:49 2008'' |
Revision as of 15:56, 21 February 2008
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THIOREDOXIN H2 (HVTRXH2) IN A MIXED DISULFIDE COMPLEX WITH THE TARGET PROTEIN BASI
Overview
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.
About this Structure
2IWT is a Protein complex structure of sequences from Hordeum vulgare with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural basis for target protein recognition by the protein disulfide reductase thioredoxin., Maeda K, Hagglund P, Finnie C, Svensson B, Henriksen A, Structure. 2006 Nov;14(11):1701-10. PMID:17098195
Page seeded by OCA on Thu Feb 21 17:56:49 2008
Categories: Hordeum vulgare | Protein complex | Finnie, C. | Hagglund, P. | Henriksen, A. | Maeda, K. | Svensson, B. | FLC | Alpha-amylase inhibitor | Amy2 | Basi | Disulfide intermediate | Disulfide reductase | Oxidoreductase | Protease inhibitor | Redox | Serine protease inhibitor | Substrate recognition | Thioredoxin
