6khx

Crystal structure of Prx from Akkermansia muciniphila

spinqualitylabelsall models 6khx, resolution 2.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6khx is a 10 chain structure with sequence from Akkermansia muciniphila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.58Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2N8HPY4_9BACT Publication Abstract from PubMed 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 alpha4 helix and beta6 strand is involved in the decameric interaction. Deletion of this loop destroys the decameric structure and significantly decreases the peroxidase activity of AmPrx. Our findingss reveal a novel regulatory mechanism of typical 2-Cys Prx, in which the alpha4-beta6 loop affects the assembly of Prx and, therefore, regulates its peroxidase activity. Crystal structure of Akkermansia muciniphila peroxiredoxin reveals a novel regulatory mechanism of typical 2-Cys Prxs by a distinct loop.,Li M, Wang J, Xu W, Wang Y, Zhang M, Wang M FEBS Lett. 2020 Feb 6. doi: 10.1002/1873-3468.13753. PMID:32027024 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Peroxiredoxin 3D structures

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