Crystal structure of geranylgeranyl pyrophosphate synthase (crtE) from Nonlabens dokdonensis DSW-6

Sangwoo Kim, Eun Jung Kim, Ji Bin Park, Seon Won Kim, Kyung Jin Kim

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Isoprenoids comprise a diverse group of natural products with a broad range of metabolic functions. Isoprenoids are synthesized from prenyl pyrophosphates by prenyltransferases that catalyze the isoprenoid chain-elongation process to different chain lengths. We hereby present the crystal structure of geranylgeranyl pyrophosphate synthase from the marine flavobacterium Nonlabens dokdonensis DSW-6 (NdGGPPS). NdGGPPS forms a hexamer composed of homodimeric trimer, and the monomeric structure is composed of 15 α-helices (α1–α15). In this structure, we observed the binding of one pyrophosphate molecule and two glycerol molecules that mimicked substrate binding to the enzyme. The substrate binding site of NdGGPPS contains large hydrophobic residues such as Phe, His and Tyr, and structural and amino acids sequence analyses thereof suggest that the protein belongs to the short-chain prenyltransferase family.

Original languageEnglish
Pages (from-to)479-485
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume518
Issue number3
DOIs
StatePublished - 20 Oct 2019

Keywords

  • GGPPS
  • Isoprenoid
  • Nonlabens dokdonensis DSW-6
  • Prenyltransferase

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