1ps1 | pdb_00001ps1
PENTALENENE SYNTHASE
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| 1ps1, resolution 2.60Å | |||||||||||||
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| Sites: | AR1 and AR2 | ||||||||||||
| Ligands: | PBM | ||||||||||||
| Activity: | Pentalenene synthase, with EC number 4.2.3.7 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.. 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 Sun Mar 30 23:03:46 2008
