6KD0
Crystal Structure of Vibralactone Cyclase
Summary for 6KD0
| Entry DOI | 10.2210/pdb6kd0/pdb |
| Descriptor | Vibralactone Cyclase (2 entities in total) |
| Functional Keywords | vibralactone cyclase, hydrolase |
| Biological source | Boreostereum vibrans |
| Total number of polymer chains | 1 |
| Total formula weight | 38718.91 |
| Authors | Zeng, Y.,Feng, K.N. (deposition date: 2019-06-30, release date: 2020-06-24, Last modification date: 2023-11-22) |
| Primary citation | Feng, K.N.,Yang, Y.L.,Xu, Y.X.,Zhang, Y.,Feng, T.,Huang, S.X.,Liu, J.K.,Zeng, Y. A Hydrolase-Catalyzed Cyclization Forms the Fused Bicyclic beta-Lactone in Vibralactone. Angew.Chem.Int.Ed.Engl., 59:7209-7213, 2020 Cited by PubMed Abstract: Vibralactone is isolated from the basidiomycete fungus Boreostereum vibrans as one of the strongest lipase inhibitors. Its unusual β-lactone-fused bicycle is derived from an aryl ring moiety by an oxidative ring-expansion prior to an intramolecular cyclization. Herein, we report the discovery of the cyclase VibC which belongs to the α/β-hydrolase superfamily and is involved in the vibralactone biosynthesis. Biochemical and crystal studies suggest that VibC may catalyze an aldol or an electrocyclic reaction initiated by the Ser-His-Asp catalytic triad. For the aldol and pericyclic chemistry in living cells, VibC is a unique hydrolase performing the carbocycle formation of an oxepinone to a fused bicyclic β-lactone. This presents a naturally occurring, new enzymatic reaction in both aldol and hydrolase (bio)chemistry that will guide future exploitation of these enzymes in synthetic biology for chemical-diversity expansion of natural products. PubMed: 32050043DOI: 10.1002/anie.202000710 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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