Crystal structure of sulfonic peroxiredoxin Ahp1 in complex with thioredoxin Trx2 mimics a conformational intermediate during the catalytic cycle
| Autor: | Xiangwei Yang, Yong-Liang Jiang, Wancai Yang, Fu-Ming Lian |
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| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Conformational change Stereochemistry Protein Conformation Thioredoxin h 02 engineering and technology Crystallography X-Ray Biochemistry Models Biological Catalysis 03 medical and health sciences Structure-Activity Relationship Structural Biology Cloning Molecular Molecular Biology Alkyl 030304 developmental biology chemistry.chemical_classification 0303 health sciences Binding Sites Chemistry Hydrogen bond General Medicine Peroxiredoxins 021001 nanoscience & nanotechnology Catalytic cycle Thiol Thioredoxin 0210 nano-technology Peroxiredoxin Oxidation-Reduction Cysteine Protein Binding |
| Zdroj: | International journal of biological macromolecules. 161 |
| ISSN: | 1879-0003 |
| Popis: | Peroxiredoxin (Prx) is a thiol-based peroxidase that eliminates reactive oxygen species to avoid oxidative damage. Alkyl hydroperoxide reductase Ahp1 is a novel and specific typical 2-cysteine Prx. Here, we present the crystal structure of sulfonic Ahp1 complexed with thioredoxin Trx2 at 2.12 A resolution. This structure implies that the transient Ahp1-Trx2 complex during the catalytic cycle already have an ability to decompose the peroxides. Structural analysis reveals that the segment glutamine23–lysine32 juxtaposed to the resolving cysteine (CR) of Ahp1 moves inward to generate a compact structure upon peroxidatic cysteine (CP) overoxidation, resulting in the breakdown of several conserved hydrogen bonds formed by Ahp1-Trx2 complex interaction. Structural comparisons suggest that the structure of sulfonic Ahp1 represents a novel conformation of Ahp1, which can mimic a conformational intermediate between the reduced and oxidized forms. Therefore, this study may provide a new structural insight into the intermediate state in which the segment glutamine23–lysine32 juxtaposed to the cysteine31 (CR) undergoes a conformational change upon cysteine62 (CP) oxidation to prepare for the formation of an intermolecular CP-CR disulfide bond during Ahp1 catalytic cycle. |
| Databáze: | OpenAIRE |
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