8HLA

Heteromeric ring comprised of peroxiredoxin from Thermococcus kodakaraensis (TkPrx) F42C/C46S/C205S/C211S mutant modified with 2-(bromoacetyl)naphthalene (Naph@TkPrx*F42C) and TkPrx C46S/F76C/C205S/C211S mutant modified with 2-(bromoacetyl)naphthalene (Naph@TkPrx*F76C) (Naph@(MIX|3:3))

8HLA の概要

• エントリーDOI: 10.2210/pdb8hla/pdb
• 関連するPDBエントリー: 8HH0
• EMDBエントリー: 34859
• 分子名称: Peroxiredoxin, 1-naphthalen-2-ylethanone (3 entities in total)
• 機能のキーワード: peroxiredoxin, complex, protein protein interactions, oxidoreductase
• 由来する生物種: Thermococcus kodakarensis KOD1; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 297064.19

構造登録者

Himiyama, T.,Hamaguchi, T.,Yonekura, K.,Nakamura, T. (登録日: 2022-11-29, 公開日: 2023-03-22, 最終更新日: 2024-11-06)

主引用文献

Himiyama, T.,Hamaguchi, T.,Yonekura, K.,Nakamura, T.
Unnaturally Distorted Hexagonal Protein Ring Alternatingly Reorganized from Two Distinct Chemically Modified Proteins.
Bioconjug.Chem., 2023

PubMed Abstract: In this study, we constructed a semiartificial protein assembly of alternating ring type, which was modified from the natural assembly state via incorporation of a synthetic component at the protein interface. For the redesign of a natural protein assembly, a scrap-and-build approach employing chemical modification was used. Two different protein dimer units were designed based on peroxiredoxin from , which originally forms a dodecameric hexagonal ring with six homodimers. The two dimeric mutants were reorganized into a ring by reconstructing the protein-protein interactions via synthetic naphthalene moieties introduced by chemical modification. Cryo-electron microscopy revealed the formation of a uniquely shaped dodecameric hexagonal protein ring with broken symmetry, distorted from the regular hexagon of the wild-type protein. The artificially installed naphthalene moieties were arranged at the interfaces of dimer units, forming two distinct protein-protein interactions, one of which is highly unnatural. This study deciphered the potential of the chemical modification technique that constructs semiartificial protein structures and assembly hardly accessible by conventional amino acid mutations.

PubMed: 36888722
DOI: 10.1021/acs.bioconjchem.3c00057

実験手法

ELECTRON MICROSCOPY (2.81 Å)