9b99 | pdb_00009b99

Crystal structure of Grindelia robusta 7,13-copalyl diphosphate synthase

spinqualitylabelsall models 9b99, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9b99 is a 1 chain structure with sequence from Grindelia hirsutula. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.12Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H4SRM2_9ASTR Publication Abstract from PubMed Diterpenoid natural products serve critical functions in plant development and ecological adaptation and many diterpenoids have economic value as bioproducts. The family of class II diterpene synthases catalyzes the committed reactions in diterpenoid biosynthesis, converting a common geranylgeranyl diphosphate precursor into different bicyclic prenyl diphosphate scaffolds. Enzymatic rearrangement and modification of these precursors generates the diversity of bioactive diterpenoids. We report the crystal structure of Grindelia robusta 7,13-copalyl diphosphate synthase, GrTPS2, at 2.1 A of resolution. GrTPS2 catalyzes the committed reaction in the biosynthesis of grindelic acid, which represents the signature metabolite in species of gumweed (Grindelia spp., Asteraceae). Grindelic acid has been explored as a potential source for drug leads and biofuel production. The GrTPS2 crystal structure adopts the conserved three-domain fold of class II diterpene synthases featuring a functional active site in the gammabeta-domain and a vestigial a-domain. Substrate docking into the active site of the GrTPS2 apo protein structure predicted catalytic amino acids. Biochemical characterization of protein variants identified residues with impact on enzyme activity and catalytic specificity. Specifically, mutagenesis of Y457 provided mechanistic insight into the position-specific deprotonation of the intermediary carbocation to form the characteristic 7,13 double bond of 7,13-copalyl diphosphate. The crystal structure of Grindelia robusta 7,13-copalyl diphosphate synthase reveals active site features controlling catalytic specificity.,Cowie AE, Pereira JH, DeGiovanni A, McAndrew RP, Palayam M, Peek JO, Muchlinski AJ, Yoshikuni Y, Shabek N, Adams PD, Zerbe P J Biol Chem. 2024 Oct 23:107921. doi: 10.1016/j.jbc.2024.107921. PMID:39454950 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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