5gul | pdb_00005gul

Crystal structure of Tris/PPix2/Mg2+ bound form of cyclolavandulyl diphosphate synthase (CLDS) from Streptomyces sp. CL190

spinqualitylabelsall models 5gul, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gul is a 4 chain structure with sequence from Streptomyces sp. CL190. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.73Å Ligands: MG, POP, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function X5IYJ5_STRC1 Publication Abstract from PubMed We report the three-dimensional structure of cyclolavandulyl diphosphate (CLPP) synthase (CLDS), which consecutively catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) followed by cyclization to form a cyclic monoterpene, CLPP. The structures of apo-CLDS and CLDS in complex with Tris, pyrophosphate, and Mg(2+) ion were refined at 2.00 A resolution and 1.73 A resolution, respectively. CLDS adopts a typical fold for cis-prenyl synthases and forms a homo-dimeric structure. An in vitro reaction using a regiospecifically (2) H-substituted DMAPP substrate revealed the intramolecular proton transfer mechanism of the CLDS reaction. The CLDS structure and structure-based mutagenesis provide mechanistic insights into this unprecedented terpene synthase. The combination of structural and mechanistic insights advances the knowledge of intricate terpene synthase-catalyzed reactions. Structure and Mechanism of the Monoterpene Cyclolavandulyl Diphosphate Synthase that Catalyzes Consecutive Condensation and Cyclization.,Tomita T, Kobayashi M, Karita Y, Yasuno Y, Shinada T, Nishiyama M, Kuzuyama T Angew Chem Int Ed Engl. 2017 Nov 20;56(47):14913-14917. doi:, 10.1002/anie.201708474. Epub 2017 Oct 11. PMID:28922556 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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