5GUL

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

Summary for 5GUL

• Entry DOI: 10.2210/pdb5gul/pdb
• Related: 5GUK
• Descriptor: Cyclolavandulyl diphosphate synthase, PYROPHOSPHATE 2-, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: cyclolavandulyl diphosphate synthase, cis-prenyltransferase, streptomyces sp. cl190, tris, ppi, mg2+, biosynthetic protein
• Biological source: Streptomyces sp. (strain CL190)
• Total number of polymer chains: 4
• Total formula weight: 108697.96

Authors

Tomita, T.,Kobayashi, M.,Nishiyama, M.,Kuzuyama, T. (deposition date: 2016-08-29, release date: 2017-08-30, Last modification date: 2023-11-08)

Primary citation

Tomita, T.,Kobayashi, M.,Karita, Y.,Yasuno, Y.,Shinada, T.,Nishiyama, M.,Kuzuyama, T.
Structure and Mechanism of the Monoterpene Cyclolavandulyl Diphosphate Synthase that Catalyzes Consecutive Condensation and Cyclization.
Angew. Chem. Int. Ed. Engl., 56:14913-14917, 2017

PubMed Abstract: 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 ion were refined at 2.00 Å resolution and 1.73 Å resolution, respectively. CLDS adopts a typical fold for cis-prenyl synthases and forms a homo-dimeric structure. An in vitro reaction using a regiospecifically 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.

PubMed: 28922556
DOI: 10.1002/anie.201708474

Experimental method

X-RAY DIFFRACTION (1.73 Å)