Crystal structure of Akkermansia muciniphila peroxiredoxin reveals a novel regulatory mechanism of typical 2‐Cys Prxs by a distinct loop. Issue 10 (20th February 2020)

• Record Type: Journal Article
• Authors: Li, Mengyu; Wang, Junchao; Xu, Wenjuan; Wang, Yongzhong; Zhang, Min; Wang, Mingzhu
• Is Part Of: FEBS letters. Volume 594:Issue 10(2020)
• Page Start: 1550
• Page End: 1563
• Publication Date: 2020-02-20
• Subjects: Akkermansia muciniphila -- antioxidant enzyme -- crystal structure -- peroxidase activity -- peroxiredoxins -- reactive oxygen species; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13753
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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 ( Am Prx) is a typical 2‐Cys Prx characterized by two conserved cysteines: Cys49 and Cys183. Here, we verified the peroxidase activity of Am Prx and determined its crystal structure in reduced form, which is a doughnut‐shaped decamer composed of five dimers. Particularly, a distinct loop between the α4 helix and β6 strand is involved in the decameric interaction. Deletion of this loop destroys the decameric structure and significantly decreases the peroxidase activity of Am Prx. Our findings reveal a novel regulatory mechanism of typical 2‐Cys Prx, in which the α4‐β6 loop affects the assembly of Prx and, therefore, regulates its peroxidase activity. Abstract :