Structural highlights
FunctionPublication Abstract from PubMedTerpene cyclases (TCs), extraordinary enzymes that create the structural diversity seen in terpene natural products, are traditionally divided into two classes, class I and class II. Although the structural and mechanistic features of class I TCs are well-known, the corresponding details in class II counterparts have not been fully characterized. Here, we report the genome mining discovery and structural characterization of two class II sesquiterpene cyclases (STCs) from Streptomyces. These drimenyl diphosphate synthases (DMSs) are the first STCs shown to possess beta,gamma-didomain architecture. High-resolution X-ray crystal structures of DMS from Streptomyces showdoensis (SsDMS) in complex with both a farnesyl diphosphate and Mg(2+) unveiled an induced-fit mechanism, with an unprecedented Mg(2+) binding mode, finally solving one of the lingering questions in class II TC enzymology. This study supports continued genome mining for novel bacterial TCs and provides new mechanistic insights into canonical class II TCs that will lead to advances in TC engineering and synthetic biology. Discovery, Structure, and Mechanism of a Class II Sesquiterpene Cyclase.,Pan X, Du W, Zhang X, Lin X, Li FR, Yang Q, Wang H, Rudolf JD, Zhang B, Dong LB J Am Chem Soc. 2022 Dec 7;144(48):22067-22074. doi: 10.1021/jacs.2c09412. Epub , 2022 Nov 23. PMID:36416740[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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