6SBF
Structure of type II terpene cyclase MstE_Y157F from Scytonema (apo)
Summary for 6SBF
| Entry DOI | 10.2210/pdb6sbf/pdb |
| Related | 6SBB |
| Descriptor | MstE, GLYCEROL, BETA-MERCAPTOETHANOL, ... (4 entities in total) |
| Functional Keywords | type ii terpene cyclase, marine drugs, merosterol, alpha6-alpha6 barrel, biosynthetic protein |
| Biological source | Scytonema sp. PCC 10023 |
| Total number of polymer chains | 1 |
| Total formula weight | 40898.72 |
| Authors | Moosmann, P.,Ecker, F.,Leopold-Messer, S.,Cahn, J.K.B.,Groll, M.,Piel, J. (deposition date: 2019-07-19, release date: 2020-07-15, Last modification date: 2024-01-24) |
| Primary citation | Moosmann, P.,Ecker, F.,Leopold-Messer, S.,Cahn, J.K.B.,Dieterich, C.L.,Groll, M.,Piel, J. A monodomain class II terpene cyclase assembles complex isoprenoid scaffolds. Nat.Chem., 12:968-972, 2020 Cited by PubMed Abstract: Class II terpene cyclases, such as oxidosqualene and squalene-hopene cyclases, catalyse some of the most complex polycyclization reactions. They minimally exhibit a β,γ-didomain architecture that has been evolutionarily repurposed in a wide range of terpene-processing enzymes and likely resulted from a fusion of unidentified monodomain proteins. Although single domain class I terpene cyclases have already been identified, the corresponding class II counterparts have not been previously reported. Here we present high-resolution X-ray structures of a monodomain class II cyclase, merosterolic acid synthase (MstE). With a minimalistic β-domain architecture, this cyanobacterial enzyme is able to construct four rings in cytotoxic meroterpenoids with a sterol-like topology. The structures with bound substrate, product, and inhibitor provide detailed snapshots of a cyclization mechanism largely governed by residues located in a noncanonical enzyme region. Our results complement the few known class II cyclase crystal structures, while also indicating that archaic monodomain cyclases might have already catalyzed complex reaction cascades. PubMed: 32778689DOI: 10.1038/s41557-020-0515-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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