1ps1
From Proteopedia
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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: and . 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 Tue Dec 18 17:51:53 2007
