Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin. / Maeda, Kenji; Hägglund, Per; Finnie, Christine; Svensson, Birte; Henriksen, Anette.

In: Structure, Vol. 14, No. 11, 2006, p. 1701-1710.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Maeda, K, Hägglund, P, Finnie, C, Svensson, B & Henriksen, A 2006, 'Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin', Structure, vol. 14, no. 11, pp. 1701-1710. https://doi.org/10.1016/j.str.2006.09.012

APA

Maeda, K., Hägglund, P., Finnie, C., Svensson, B., & Henriksen, A. (2006). Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin. Structure, 14(11), 1701-1710. https://doi.org/10.1016/j.str.2006.09.012

Vancouver

Maeda K, Hägglund P, Finnie C, Svensson B, Henriksen A. Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin. Structure. 2006;14(11):1701-1710. https://doi.org/10.1016/j.str.2006.09.012

Author

Maeda, Kenji ; Hägglund, Per ; Finnie, Christine ; Svensson, Birte ; Henriksen, Anette. / Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin. In: Structure. 2006 ; Vol. 14, No. 11. pp. 1701-1710.

Bibtex

@article{0bc9469fba114ce0b4da4acd1dcdf886,
title = "Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin",
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 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.",
keywords = "PROTEINS",
author = "Kenji Maeda and Per H{\"a}gglund and Christine Finnie and Birte Svensson and Anette Henriksen",
year = "2006",
doi = "10.1016/j.str.2006.09.012",
language = "English",
volume = "14",
pages = "1701--1710",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "11",

}

RIS

TY - JOUR

T1 - Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin

AU - Maeda, Kenji

AU - Hägglund, Per

AU - Finnie, Christine

AU - Svensson, Birte

AU - Henriksen, Anette

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

KW - PROTEINS

U2 - 10.1016/j.str.2006.09.012

DO - 10.1016/j.str.2006.09.012

M3 - Journal article

C2 - 17098195

AN - SCOPUS:33846393586

VL - 14

SP - 1701

EP - 1710

JO - Structure

JF - Structure

SN - 0969-2126

IS - 11

ER -

ID: 240161387