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A Prospective Target for Advanced Biofuel Production Print
Thursday, 02 February 2012 13:34

The sesquiterpene bisabolene was recently identified as a biosynthetic precursor to bisabolane, an advanced biofuel with physico-chemical properties similar to D2 diesel. High titer microbial bisabolene production was achieved using Abies grandis α-bisabolene synthase (AgBIS). Researchers have determined 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 led researchers to propose a catalytic mechanism for the cyclization of farnesyl diphosphate into bisabolene via a bisabolyl cation intermediate. Further, this paper describes the non-functional 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.

 

 

The structure of AgBIS is composed of three distinct α-helical domains. The α domain (cyan) hosts the terpene synthase Class I active site, which is characterized by the presence of the conserved metal binding motifs. Farnesyl thiophosphate and Mg2+ ions are represented as magenta sticks and green spheres, respectively.

 


 

Work performed on ALS Beamlines 5.0.38.2.1, and 8.2.2.

Citation: R.P. McAndrew, P.P. Peralta-Yahya, A. DeGiovanni, J.H. Pereira, M.Z. Hadi, J.D. Keasling, and P. D. Adams, "Structure of a three-domain sesquiterpene synthase: a prospective target for advanced biofuels production," Structure 19, 1876-1884 (2011). DOI: 10.1016/j.str.2011.09.013