1ps1: Difference between revisions

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==Overview==
==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.
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==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptomyces sp.]]
[[Category: Streptomyces sp.]]
[[Category: Transferred entry: 4.2.3.7]]
[[Category: Transferred entry: 4 2.3 7]]
[[Category: Christianson, D.W.]]
[[Category: Christianson, D W.]]
[[Category: Lesburg, C.A.]]
[[Category: Lesburg, C A.]]
[[Category: PBM]]
[[Category: PBM]]
[[Category: antibiotic biosynthesis]]
[[Category: antibiotic biosynthesis]]
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[[Category: sesquiterpene cyclase]]
[[Category: sesquiterpene cyclase]]


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