9rs2

Sesterterpene Synthase from Kitasatospora viridis in complex with the surrogate GFSPP

spinqualitylabelsall models 9rs2, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9rs2 is a 2 chain structure with sequence from Kitasatospora. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: A1JI6, EDO, GOL, MG, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A561SAF2_9ACTN Publication Abstract from PubMed 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. Structure-Guided Engineering of a Bacterial Sesterterpene Synthase for Sesterviridene Diversification.,Li H, Troycke P, Yin Z, Groll M, Dickschat JS J Am Chem Soc. 2025 Sep 11. doi: 10.1021/jacs.5c11309. PMID:40931719 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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