1PS1

PENTALENENE SYNTHASE

Summary for 1PS1

• Entry DOI: 10.2210/pdb1ps1/pdb
• Descriptor: PENTALENENE SYNTHASE, TRIMETHYL LEAD ION (3 entities in total)
• Functional Keywords: antibiotic biosynthesis, sesquiterpene cyclase, lyase
• Biological source: Streptomyces sp.
• Total number of polymer chains: 2
• Total formula weight: 76353.13

Authors

Lesburg, C.A.,Christianson, D.W. (deposition date: 1997-03-23, release date: 1998-03-25, Last modification date: 2024-11-20)

Primary citation

Lesburg, C.A.,Zhai, G.,Cane, D.E.,Christianson, D.W.
Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.
Science, 277:1820-1824, 1997

PubMed Abstract: 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.

PubMed: 9295272
DOI: 10.1126/science.277.5333.1820

Experimental method

X-RAY DIFFRACTION (2.6 Å)