5GUK

Crystal structure of apo form of cyclolavandulyl diphosphate synthase (CLDS) from Streptomyces sp. CL190

5GUK の概要

• エントリーDOI: 10.2210/pdb5guk/pdb
• 関連するPDBエントリー: 5GUL
• 分子名称: Cyclolavandulyl diphosphate synthase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: cyclolavandulyl diphosphate synthase, cis-prenyltransferase, apo form, streptomyces sp. cl190, biosynthetic protein
• 由来する生物種: Streptomyces sp. (strain CL190)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50483.86

構造登録者

Tomita, T.,Kobayashi, M.,Nishiyama, M.,Kuzuyama, T. (登録日: 2016-08-29, 公開日: 2017-08-30, 最終更新日: 2024-03-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)