Monoterpene Synthase Structural Modeling
Three-dimensional Structure of the 3 Terpene Synthase Proteins
Reactive site of the alpha-pinene synthase
List of Amino Acid Residues in Alpha-Pinene Synthase Within 3.5 Angstrom of the Reactive Site
606G, 609Q, 610V, 613D, 710Y, 714V, 715G, 719C, 753W, 754R, 757N, 765E, 770Q
We propose that these sites are important to terpene synthesis.
Materials and Methods
We used MODELLER (1) to automate homology-based 3D structure prediction. We identified an experimentally determined 3D structure of a taxadiene synthase from Pacific Yew (PDB ID: 3P5R) as an appropriate template for modeling. The substrate GDP was docked using functions implemented in ICM by Molsoft LLC (2). All images were taken using the ICM by Molsoft LLC.
Future DirectionsIn the current study, we identified putative amino acid residues that may be important to the efficient of terpene synthesis. We propose that these amino acid sites can be mutated in the future to create mutant versions of the terpene synthases that exhibit greater terpene production output.
References1. N. Eswar, M. A. Marti-Renom, B. Webb, M. S. Madhusudhan, D. Eramian, M. Shen, U. Pieper, A. Sali. Comparative Protein Structure Modeling With MODELLER. Current Protocols in Bioinformatics, John Wiley & Sons, Inc., Supplement 15, 5.6.1-5.6.30, 2006.
2. Abagyan, R.A., Totrov, M.M., and Kuznetsov, D.A. Icm: A New Method For Protein Modeling and Design: Applications To Docking and Structure Prediction From The Distorted Native Conformation. J. Comp. Chem. 15, 488-506. 1994.
We are very grateful to Yvonne Y. Li from the BC Genome Sciences Centre for valuable technical advice.