3SDR

Structure of a three-domain sesquiterpene synthase: a prospective target for advanced biofuels production

3SDR の概要

• エントリーDOI: 10.2210/pdb3sdr/pdb
• 関連するPDBエントリー: 3SAE 3SDQ 3SDT 3SDU 3SDV
• 分子名称: Alpha-bisabolene synthase, CHLORIDE ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: lyase, terpene synthase
• 由来する生物種: Abies grandis (grand fir,lowland fir,lowland white fir,silver fir,white fir,yellow fir)
• 細胞内の位置: Cytoplasm (Probable): O81086
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 94198.58

構造登録者

McAndrew, R.P.,Peralta-Yahya, P.P.,DeGiovanni, A.,Pereira, J.H.,Hadi, M.Z.,Keasling, J.D.,Adams, P.D. (登録日: 2011-06-09, 公開日: 2011-12-14, 最終更新日: 2024-02-28)

主引用文献

McAndrew, R.P.,Peralta-Yahya, P.P.,DeGiovanni, A.,Pereira, J.H.,Hadi, M.Z.,Keasling, J.D.,Adams, P.D.
Structure of a three-domain sesquiterpene synthase: a prospective target for advanced biofuels production.
Structure, 19:1876-1884, 2011

PubMed Abstract: The sesquiterpene bisabolene was recently identified as a biosynthetic precursor to bisabolane, an advanced biofuel with physicochemical properties similar to those of D2 diesel. High-titer microbial bisabolene production was achieved using Abies grandis α-bisabolene synthase (AgBIS). Here, we report the structure of AgBIS, a three-domain plant sesquiterpene synthase, crystallized in its apo form and bound to five different inhibitors. Structural and biochemical characterization of the AgBIS terpene synthase Class I active site leads us to propose a catalytic mechanism for the cyclization of farnesyl diphosphate into bisabolene via a bisabolyl cation intermediate. Further, we describe the nonfunctional AgBIS Class II active site whose high similarity to bifunctional diterpene synthases makes it an important link in understanding terpene synthase evolution. Practically, the AgBIS crystal structure is important in future protein engineering efforts to increase the microbial production of bisabolene.

PubMed: 22153510
DOI: 10.1016/j.str.2011.09.013

実験手法

X-RAY DIFFRACTION (1.86 Å)