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


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.

SUBMITTER: Kopec J 

PROVIDER: S-EPMC3212358 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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

Kopec Jolanta J   Schnell Robert R   Schneider Gunter G  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110924 Pt 10


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 enzym  ...[more]

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