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7WIJ

Cryo-EM structure of prenyltransferase domain of Macrophoma phaseolina macrophomene synthase

Summary for 7WIJ
Entry DOI10.2210/pdb7wij/pdb
EMDB information32531
DescriptorGeranylgeranyl diphosphate synthase (1 entity in total)
Functional Keywordsmacrophoma phaseolina, macrophomene synthase, prenyltransferase, transferase
Biological sourceMacrophomina phaseolina MS6
Total number of polymer chains6
Total formula weight482655.98
Authors
Mori, T.,Adachi, N.,Abe, I. (deposition date: 2022-01-03, release date: 2022-06-22, Last modification date: 2024-06-26)
Primary citationTao, 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, J.S.,Liu, T.
Discovery of non-squalene triterpenes.
Nature, 606:414-419, 2022
Cited by
PubMed Abstract: All known triterpenes are generated by triterpene synthases (TrTSs) from squalene or oxidosqualene. This approach is fundamentally different from the biosynthesis of short-chain (C-C) terpenes that are formed from polyisoprenyl diphosphates. 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.
PubMed: 35650436
DOI: 10.1038/s41586-022-04773-3
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.17 Å)
Structure validation

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