1ps1 | pdb_00001ps1
PENTALENENE SYNTHASE
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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 Structure known Active 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
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