5Y7R
Quaternary complex of AsqJ-Fe3+-2OG-cyclopeptin
Summary for 5Y7R
| Entry DOI | 10.2210/pdb5y7r/pdb |
| Descriptor | Iron/alpha-ketoglutarate-dependent dioxygenase asqJ, FE (III) ION, 2-OXOGLUTARIC ACID, ... (5 entities in total) |
| Functional Keywords | initial step for olefination, oxidoreductase |
| Biological source | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) |
| Total number of polymer chains | 1 |
| Total formula weight | 34505.24 |
| Authors | Liao, H.J.,Lin, T.S. (deposition date: 2017-08-17, release date: 2018-01-24, Last modification date: 2024-03-27) |
| Primary citation | Liao, H.J.,Li, J.,Huang, J.L.,Davidson, M.,Kurnikov, I.,Lin, T.S.,Lee, J.L.,Kurnikova, M.,Guo, Y.,Chan, N.L.,Chang, W.C. Insights into the Desaturation of Cyclopeptin and its C3 Epimer Catalyzed by a non-Heme Iron Enzyme: Structural Characterization and Mechanism Elucidation. Angew. Chem. Int. Ed. Engl., 57:1831-1835, 2018 Cited by PubMed Abstract: AsqJ, an iron(II)- and 2-oxoglutarate-dependent enzyme found in viridicatin-type alkaloid biosynthetic pathways, catalyzes sequential desaturation and epoxidation to produce cyclopenins. Crystal structures of AsqJ bound to cyclopeptin and its C3 epimer are reported. Meanwhile, a detailed mechanistic study was carried out to decipher the desaturation mechanism. These findings suggest that a pathway involving hydrogen atom abstraction at the C10 position of the substrate by a short-lived Fe -oxo species and the subsequent formation of a carbocation or a hydroxylated intermediate is preferred during AsqJ-catalyzed desaturation. PubMed: 29314482DOI: 10.1002/anie.201710567 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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