7BVV

Crystal structure of sulfonic peroxiredoxin Ahp1 in complex with thioredoxin Trx2

Summary for 7BVV

• Entry DOI: 10.2210/pdb7bvv/pdb
• Descriptor: Peroxiredoxin AHP1, Thioredoxin-2 (3 entities in total)
• Functional Keywords: peroxiredoxin, thioredoxin, alkyl hydroperoxide reductase, complex, oxidoreductase
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 31395.50

Authors

Lian, F.M.,Jiang, Y.L.,Yang, W.,Yang, X. (deposition date: 2020-04-11, release date: 2020-07-01, Last modification date: 2023-11-29)

Primary citation

Lian, F.M.,Jiang, Y.L.,Yang, W.,Yang, X.
Crystal structure of sulfonic peroxiredoxin Ahp1 in complex with thioredoxin Trx2 mimics a conformational intermediate during the catalytic cycle.
Int.J.Biol.Macromol., 161:1055-1060, 2020

PubMed 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 Å 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 (C) of Ahp1 moves inward to generate a compact structure upon peroxidatic cysteine (C) 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 (C) undergoes a conformational change upon cysteine62 (C) oxidation to prepare for the formation of an intermolecular C-C disulfide bond during Ahp1 catalytic cycle.

PubMed: 32531362
DOI: 10.1016/j.ijbiomac.2020.06.065

Experimental method

X-RAY DIFFRACTION (2.12 Å)