Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis

Biochem Biophys Res Commun. 2018 Jan 8;495(2):1782-1788. doi: 10.1016/j.bbrc.2017.12.039. Epub 2017 Dec 8.

Abstract

FamD1 is a novel CloQ/NphB-family indole prenyltransferase which involves in hapalindole-type alkaloid biosynthesis. Here the native FamD1 structure and three protein-ligand complexes are analyzed to investigate the molecular basis of substrate binding and catalysis. FamD1 adopts a typical ABBA architecture of aromatic prenyltransferase, in which the substrate-binding chamber is found in the central β-barrel. The indole-containing acceptor substrate is bound adjacent to the prenyl donor. Based on the complex structures, a catalytic mechanism of FamD1 is proposed. Functional implications on the sister enzyme FamD2 are also discussed.

Keywords: Aromatic prenyltransferase; Crystal structure; FamD1; Stigonematales.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Cyanobacteria / enzymology
  • Cyanobacteria / genetics
  • Dimethylallyltranstransferase / chemistry*
  • Dimethylallyltranstransferase / genetics
  • Dimethylallyltranstransferase / metabolism*
  • Indole Alkaloids / chemistry
  • Indole Alkaloids / metabolism*
  • Models, Molecular
  • Protein Conformation
  • Protein Folding
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism

Substances

  • Bacterial Proteins
  • Indole Alkaloids
  • Recombinant Proteins
  • Dimethylallyltranstransferase