9RS4
Sesterterpene Synthase from Kitasatospora viridis (V57L-Variant, apo)
Summary for 9RS4
| Entry DOI | 10.2210/pdb9rs4/pdb |
| Descriptor | Terpene synthase, GLYCEROL (3 entities in total) |
| Functional Keywords | type i terpene synthases, terpene cyclization mechanism, carbocation cascade, enzyme engineering, active site mutagenesis, chemodiversity, lyase |
| Biological source | Kitasatospora viridis |
| Total number of polymer chains | 1 |
| Total formula weight | 39913.96 |
| Authors | Li, H.,Troycke, P.,Yin, Z.,Groll, M.,Dickschat, J.S. (deposition date: 2025-06-30, release date: 2025-09-24, Last modification date: 2025-10-08) |
| Primary citation | Li, H.,Troycke, P.,Yin, Z.,Groll, M.,Dickschat, J.S. Structure-Guided Engineering of a Bacterial Sesterterpene Synthase for Sesterviridene Diversification. J.Am.Chem.Soc., 147:34901-34909, 2025 Cited by PubMed Abstract: Terpene synthases produce a remarkable structural diversity from acyclic precursors through complex carbocation cascades. Here, we report the crystal structure of the bacterial sesterterpene synthase StvirS bound to geranylfarnesyl thiopyrophosphate (GFSPP), revealing a preorganized active site that enforces a defined folding of the C25 backbone. Guided by this structure, active-site engineering at 11 positions yielded 23 enzyme variants and 13 new sesterterpenes. Specific substitutions altered reaction trajectories, stereochemistry, or induced premature termination, emphasizing the sensitivity of StvirS to subtle structural changes. Isotopic labeling established the absolute configurations of 11 products and experimentally confirmed a conserved cyclization pathway. These results illustrate how precise noncovalent interactions govern terpene biosynthesis and highlight the promise of structure-based design to reprogram terpene cyclase reactivity. PubMed: 40931719DOI: 10.1021/jacs.5c11309 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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