1ps1 | pdb_00001ps1
PENTALENENE SYNTHASE
|
Overview
The crystal structure of pentalenene synthase at 2.6 angstrom resolution reveals critical active site features responsible for the cyclization of farnesyl diphosphate into the tricyclic hydrocarbon pentalenene. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. The core active site structure of the enzyme may be preserved among the greater family of terpenoid synthases, possibly implying divergence from a common ancestral synthase to satisfy biological requirements for increasingly diverse natural products.
About this Structure
1PS1 is a Single protein structure of sequence from Streptomyces sp. with PBM as ligand. Active as Transferred entry: 4.2.3.7, with EC number 4.6.1.5 Known structural/functional Sites: AR1 and AR2. Full crystallographic information is available from OCA.
Reference
Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology., Lesburg CA, Zhai G, Cane DE, Christianson DW, Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272
Page seeded by OCA on Thu Feb 21 14:32:00 2008
