Open AccessStructure of PA4019, a putative aromatic acid decarboxylase from Pseudomonas aeruginosa
Author(s) -
Kopec Jolanta,
Schnell Robert,
Schneider Gunter
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911102923x
Subject(s) - biochemistry , protein subunit , biology , mutagenesis , gene , enzyme , cysteine , chemistry , mutant
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.