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Crystal structure of sulfonic peroxiredoxin Ahp1 in complex with thioredoxin Trx2 mimics a conformational intermediate during the catalytic cycle
- Source :
- International journal of biological macromolecules. 161
- Publication Year :
- 2020
-
Abstract
- 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.
- Subjects :
- 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
Subjects
Details
- ISSN :
- 18790003
- Volume :
- 161
- Database :
- OpenAIRE
- Journal :
- International journal of biological macromolecules
- Accession number :
- edsair.doi.dedup.....71aceb45be0621f74f851f09729ffe13