7C87

Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) C50S/F80C/C207S/C213S mutant (ApPrx*F80C)

Summary for 7C87

• Entry DOI: 10.2210/pdb7c87/pdb
• Descriptor: Peroxiredoxin, CITRIC ACID (3 entities in total)
• Functional Keywords: peroxiredoxin, oxidoreductase
• Biological source: Aeropyrum pernix K1
• Total number of polymer chains: 10
• Total formula weight: 288439.21

Authors

Himiyama, T.,Nakamura, T. (deposition date: 2020-05-29, release date: 2020-12-30, Last modification date: 2023-11-29)

Primary citation

Himiyama, T.,Tsuchiya, Y.,Yonezawa, Y.,Nakamura, T.
Rebuilding Ring-Type Assembly of Peroxiredoxin by Chemical Modification.
Bioconjug.Chem., 32:153-160, 2021

PubMed Abstract: Direct control of the protein quaternary structure (QS) is challenging owing to the complexity of the protein structure. As a protein with a characteristic QS, peroxiredoxin from K1 (ApPrx) forms a decamer, wherein five dimers associate to form a ring. Here, we disrupted and reconstituted ApPrx QS via amino acid mutations and chemical modifications targeting hot spots for protein assembly. The decameric QS of an ApPrx* mutant, wherein all cysteine residues in wild-type ApPrx were mutated to serine, was destructed to dimers via an F80C mutation. The dimeric ApPrx*F80C mutant was then modified with a small molecule and successfully assembled as a decamer. Structural analysis confirmed that an artificially installed chemical moiety potentially facilitates suitable protein-protein interactions to rebuild a native structure. Rebuilding of dodecamer was also achieved through an additional amino acid mutation. This study describes a facile method to regulate the protein assembly state.

PubMed: 33334100
DOI: 10.1021/acs.bioconjchem.0c00587

Experimental method

X-RAY DIFFRACTION (2.2 Å)