7de2 | pdb_00007de2

iron and alpha-ketoglutarate-dependent endoperoxidase NvfI

spinqualitylabelsall models 7de2, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7de2 is a 2 chain structure with sequence from Aspn1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AKG, FE, H3X Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Endoperoxide-containing natural products are a group of compounds with structurally unique cyclized peroxide moieties. Although numerous endoperoxide-containing compounds have been isolated, the biosynthesis of the endoperoxides remains unclear. NvfI from Aspergillus novofumigatus IBT 16806 is an endoperoxidase that catalyzes the formation of fumigatonoid A in the biosynthesis of novofumigatonin. Here, we describe our structural and functional analyses of NvfI. The structural elucidation and mutagenesis studies indicate that NvfI does not utilize a tyrosyl radical in the reaction, in contrast to other characterized endoperoxidases. Further, the crystallographic analysis reveals significant conformational changes of two loops upon substrate binding, which suggests a dynamic movement of active site during the catalytic cycle. As a result, NvfI installs three oxygen atoms onto a substrate in a single enzyme turnover. Based on these results, we propose a mechanism for the NvfI-catalyzed, unique endoperoxide formation reaction to produce fumigatonoid A. Molecular insights into the endoperoxide formation by Fe(II)/alpha-KG-dependent oxygenase NvfI.,Mori T, Zhai R, Ushimaru R, Matsuda Y, Abe I Nat Commun. 2021 Jul 20;12(1):4417. doi: 10.1038/s41467-021-24685-6. PMID:34285212 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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