Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii

Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1472-9. doi: 10.1107/S2053230X1402130X. Epub 2014 Oct 25.

Abstract

Prior studies have indicated that MJ1099 from Methanocaldococcus jannaschii has roles in the biosynthesis of tetrahydromethanopterin and methanofuran, two key cofactors of one-carbon (C1) metabolism in diverse organisms including the methanogenic archaea. Here, the structure of MJ1099 has been solved to 1.7 Å resolution using anomalous scattering methods. The results indicate that MJ1099 is a member of the TIM-barrel superfamily and that it is a homohexamer. Bioinformatic analyses identified a potential active site that is highly conserved among MJ1099 homologs and the key amino acids involved were identified. The results presented here should guide further studies of MJ1099 including mechanistic studies and possibly the development of inhibitors that target the methanogenic archaea in the digestive tracts of humans and that are a source of the greenhouse gas methane.

Keywords: MJ1099; Methanocaldococcus jannaschii; methanofuran; methanopterin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Binding Sites / physiology
  • Crystallography
  • Furans / chemistry*
  • Furans / metabolism
  • Methanocaldococcus / enzymology*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Pterins / chemistry*
  • Pterins / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • Bacterial Proteins
  • Furans
  • Pterins
  • Recombinant Proteins
  • methanopterin
  • carbon dioxide reduction factor

Associated data

  • PDB/4RC1
  • PDB/4U9P