Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue
| Autor: | Daniel Stephan, Mareike Kurz, Stephen R. Shouldice, Begonña Heras, Russell Jarrott, Annie Hiniker, Danming Tang, Guoping Ren, Zhaohui Xu, Jennifer L. Martin, Rosemary S. Harrison, Ying Zheng, James C.A. Bardwell |
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| Rok vydání: | 2009 |
| Předmět: |
Protein Folding
Proline Protein Conformation Molecular Sequence Data Molecular Conformation Protein Disulfide-Isomerases Thioredoxin fold Biochemistry Protein Structure Secondary Residue (chemistry) Thioredoxins Protein structure Escherichia coli Amino Acid Sequence Isoleucine Protein disulfide-isomerase Molecular Biology Peptide sequence Enzyme Catalysis and Regulation Chemistry Escherichia coli Proteins Ferredoxin-thioredoxin reductase Cell Biology Hydrogen-Ion Concentration Kinetics Protein folding Thioredoxin Oxidoreductases Oxidation-Reduction |
| Zdroj: | The Journal of Biological Chemistry |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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