Structure of PA4019, a putative aromatic acid decarboxylase from Pseudomonas aeruginosa

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1184-8. doi: 10.1107/S174430911102923X. Epub 2011 Sep 24.

Abstract

The ubiX gene (PA4019) of Pseudomonas aeruginosa has been annotated as encoding a putative 3-octaprenyl-4-hydroxybenzoate decarboxylase from the ubiquinone-biosynthesis pathway. Based on a transposon mutagenesis screen, this gene was also implicated as being essential for the survival of this organism. The crystal structure of recombinant UbiX determined to 1.5 Å resolution showed that the protein belongs to the superfamily of homo-oligomeric flavine-containing cysteine decarboxylases. The enzyme assembles into a dodecamer with 23 point symmetry. The subunit displays a typical Rossmann fold and contains one FMN molecule bound at the interface between two subunits.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carboxy-Lyases / chemistry*
  • Carboxy-Lyases / metabolism
  • Crystallography, X-Ray
  • Flavin Mononucleotide / chemistry
  • Flavin Mononucleotide / metabolism
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Protein Subunits / chemistry
  • Pseudomonas aeruginosa / enzymology*
  • Structural Homology, Protein

Substances

  • Protein Subunits
  • Flavin Mononucleotide
  • Carboxy-Lyases

Associated data

  • PDB/3ZQU