7vtb

Partially closed conformation of talaropentaene synthase cyclase domain

spinqualitylabelsall models 7vtb, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7vtb is a 1 chain structure with sequence from Talaromyces verruculosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed All known triterpenes are generated by triterpene synthases (TrTSs) from squalene or oxidosqualene(1). This approach is fundamentally different from the biosynthesis of short-chain (C10-C25) terpenes that are formed from polyisoprenyl diphosphates(2-4). In this study, two fungal chimeric class I TrTSs, Talaromyces verruculosus talaropentaene synthase (TvTS) and Macrophomina phaseolina macrophomene synthase (MpMS), were characterized. Both enzymes use dimethylallyl diphosphate and isopentenyl diphosphate or hexaprenyl diphosphate as substrates, representing the first examples, to our knowledge, of non-squalene-dependent triterpene biosynthesis. The cyclization mechanisms of TvTS and MpMS and the absolute configurations of their products were investigated in isotopic labelling experiments. Structural analyses of the terpene cyclase domain of TvTS and full-length MpMS provide detailed insights into their catalytic mechanisms. An AlphaFold2-based screening platform was developed to mine a third TrTS, Colletotrichum gloeosporioides colleterpenol synthase (CgCS). Our findings identify a new enzymatic mechanism for the biosynthesis of triterpenes and enhance understanding of terpene biosynthesis in nature. Discovery of non-squalene triterpenes.,Tao H, Lauterbach L, Bian G, Chen R, Hou A, Mori T, Cheng S, Hu B, Lu L, Mu X, Li M, Adachi N, Kawasaki M, Moriya T, Senda T, Wang X, Deng Z, Abe I, Dickschat JS, Liu T Nature. 2022 Jun;606(7913):414-419. doi: 10.1038/s41586-022-04773-3. Epub 2022, Jun 1. PMID:35650436 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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