Crystal structure of Akkermansiamuciniphila peroxiredoxin reveals a novel regulatory mechanism of typical 2-Cys Prxs by a distinct loop

FEBS Letters

article

Mengyu Li¹  Junchao Wang¹  Wenjuan Xu¹  Yongzhong Wang¹  Min Zhang¹  Mingzhu Wang¹ 

[1] School of Life Sciences, Anhui University;Institutes of Physical Science and Information Technology, Anhui University;Key Laboratory of Human Microenvironment and Precision Medicine of Anhui Higher Education Institutes, Anhui University

关键词: Akkermansia muciniphila;    antioxidant enzyme;    crystal structure;    peroxidase activity;    peroxiredoxins;    reactive oxygen species;   

DOI  :  10.1002/1873-3468.13753

来源: John Wiley & Sons Ltd.

【 摘 要 】

Peroxiredoxins (Prxs) are thiol-specific antioxidant proteins commonly found in organisms that protect cells from the damage of reactive oxygen species produced by metabolism and that participate in cell signaling. The Prx from the bacterium Akkermansia muciniphila (AmPrx) is a typical 2-Cys Prx characterized by two conserved cysteines: Cys49 and Cys183. Here, we verified the peroxidase activity of AmPrx and determined its crystal structure in reduced form, which is a doughnut-shaped decamer composed of five dimers. Particularly, a distinct loop between the a4 helix and b6 strand is involved in the decameric interaction. Deletion of this loop destroys the decameric structure and significantly decreases the peroxidase activity of AmPrx. Our findings reveal a novel regulatory mechanism of typical 2-Cys Prx, in which the a4-b6 loop affects the assembly of Prx and, therefore, regulates its peroxidase activity.

【 授权许可】

Unknown