Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue

Ren, G. P., Stephan, D., Xu, Z. H., Zheng, Y., Tang, D. M., Harrison, R. S., Kurz, M, Jarrott, R, Shouldice, S. R., Hiniker, A., Martin, J. L., Heras, B. and Bardwell, J. C. A. (2009) Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. Journal of Biological Chemistry, 284 15: 10150-10159. doi:10.1074/jbc.M809509200

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Author Ren, G. P.
Stephan, D.
Xu, Z. H.
Zheng, Y.
Tang, D. M.
Harrison, R. S.
Kurz, M
Jarrott, R
Shouldice, S. R.
Hiniker, A.
Martin, J. L.
Heras, B.
Bardwell, J. C. A.
Title Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2009-04
Year available 2009
Sub-type Article (original research)
DOI 10.1074/jbc.M809509200
Open Access Status File (Publisher version)
Volume 284
Issue 15
Start page 10150
End page 10159
Total pages 10
Place of publication Bethesda, MD, U. S. A.
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2010
Language eng
Subject C1
970106 Expanding Knowledge in the Biological Sciences
060112 Structural Biology (incl. Macromolecular Modelling)
0601 Biochemistry and Cell Biology
060107 Enzymes
Abstract The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold proteins but distant in sequence. This residue is just N-terminal to the conservative cis-proline. It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins.
Keyword Protein disulfide-isomerase
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes First published online 30 January, 2009

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 60 times in Thomson Reuters Web of Science Article | Citations
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Created: Thu, 03 Sep 2009, 08:24:49 EST by Mr Andrew Martlew on behalf of Institute for Molecular Bioscience