1ps1

PENTALENENE SYNTHASE

spinqualitylabelsall models 1ps1, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ps1 is a 2 chain structure with sequence from Streptomyces exfoliatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: PBM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PENA_STREX Catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene, which is the hydrocarbon precursor of the pentalenolactone family of antibiotics produced by a variety of Streptomyces species. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of pentalenene synthase at 2.6 angstrom resolution reveals critical active site features responsible for the cyclization of farnesyl diphosphate into the tricyclic hydrocarbon pentalenene. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. The core active site structure of the enzyme may be preserved among the greater family of terpenoid synthases, possibly implying divergence from a common ancestral synthase to satisfy biological requirements for increasingly diverse natural products. Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.,Lesburg CA, Zhai G, Cane DE, Christianson DW Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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