3ZLP

Crystal structure of Schistosoma mansoni Peroxiredoxin 1 C48P mutant form with four decamers in the asymmetric unit

3ZLP の概要

• エントリーDOI: 10.2210/pdb3zlp/pdb
• 関連するPDBエントリー: 3ZL5
• 分子名称: THIOREDOXIN PEROXIDASE (1 entity in total)
• 機能のキーワード: oxidoreductase, peroxidase, schistosomiasis, chaperone, thioredoxin fold
• 由来する生物種: SCHISTOSOMA MANSONI
• タンパク質・核酸の鎖数: 40
• 化学式量合計: 846603.36

構造登録者

Saccoccia, F.,Angelucci, F.,Ardini, M.,Boumis, G.,Brunori, M.,DiLeandro, L.,Ippoliti, R.,Miele, A.E.,Natoli, G.,Scotti, S.,Bellelli, A. (登録日: 2013-02-04, 公開日: 2013-09-11, 最終更新日: 2023-12-20)

主引用文献

Angelucci, F.,Saccoccia, F.,Ardini, M.,Boumis, G.,Brunori, M.,Dileandro, L.,Ippoliti, R.,Miele, A.E.,Natoli, G.,Scotti, S.,Bellelli, A.
Switching between the Alternative Structures and Functions of a 2-Cys Peroxiredoxin, by Site-Directed Mutagenesis
J.Mol.Biol., 425:4556-, 2013

PubMed Abstract: Members of the typical 2-Cys peroxiredoxin (Prx) subfamily represent an intriguing example of protein moonlighting behavior since this enzyme shifts function: indeed, upon chemical stimuli, such as oxidative stress, Prx undergoes a switch from peroxidase to molecular chaperone, associated to a change in quaternary structure from dimers/decamers to higher-molecular-weight (HMW) species. In order to detail the structural mechanism of this switch at molecular level, we have designed and expressed mutants of peroxiredoxin I from Schistosoma mansoni (SmPrxI) with constitutive HMW assembly and molecular chaperone activity. By a combination of X-ray crystallography, transmission electron microscopy and functional experiments, we defined the structural events responsible for the moonlighting behavior of 2-Cys Prx and we demonstrated that acidification is coupled to local structural variations localized at the active site and a change in oligomerization to HMW forms, similar to those induced by oxidative stress. Moreover, we suggest that the binding site of the unfolded polypeptide is at least in part contributed by the hydrophobic surface exposed by the unfolding of the active site. We also find an inverse correlation between the extent of ring stacking and molecular chaperone activity that is explained assuming that the binding occurs at the extremities of the nanotube, and the longer the nanotube is, the lesser the ratio binding sites/molecular mass is.

PubMed: 24021815
DOI: 10.1016/J.JMB.2013.09.002

実験手法

X-RAY DIFFRACTION (3.515 Å)