Structure and mechanism of an arabidopsis medium/long-chain-length prenyl pyrophosphate synthase

Fu Lien Hsieh, Tao Hsin Chang, Tzu Ping Ko, Andrew H.J. Wang

Research output: Contribution to journalArticlepeer-review

64 Citations (Scopus)


Prenyltransferases (PTSs) are involved in the biosynthesis of terpenes with diverse functions. Here, a novel PTS from Arabidopsis (Arabidopsis thaliana) is identified as a trans-type polyprenyl pyrophosphate synthase (AtPPPS), which forms a trans-double bond during each homoallylic substrate condensation, rather than a homomeric C10-geranyl pyrophosphate synthase as originally proposed. Biochemical and genetic complementation analyses indicate that AtPPPS synthesizes C25 to C45 medium/long-chain products. Its close relationship to other long-chain PTSs is also uncovered by phylogenetic analysis. A mutant of contiguous surface polar residues was produced by replacing four charged surface amino acids with alanines to facilitate the crystallization of the enzyme. The crystal structures of AtPPPS determined here in apo and ligand-bound forms further reveal an active-site cavity sufficient to accommodate the medium/long-chain products. The two monomers in each dimer adopt different conformations at the entrance of the active site depending on the binding of substrates. Taken together, these results suggest that AtPPPS is endowed with a unique functionality among the known PTSs.

Original languageEnglish
Pages (from-to)1079-1090
Number of pages12
JournalPlant Physiology
Issue number3
Publication statusPublished - Mar 2011
Externally publishedYes

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science


Dive into the research topics of 'Structure and mechanism of an arabidopsis medium/long-chain-length prenyl pyrophosphate synthase'. Together they form a unique fingerprint.

Cite this