title: 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.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden.
authors.forename: Jolanta
authors.initials: J
authors.lastname: Kopec
authors.forename: Robert
authors.initials: R
authors.lastname: Schnell
authors.forename: Gunter
authors.initials: G
authors.lastname: Schneider
mesh_terms: D002262:Carboxy-Lyases / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D005486:Flavin Mononucleotide / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D040681:Structural Homology, Protein
chemical_list: D021122:Protein Subunits; D005486:Flavin Mononucleotide; D002262:Carboxy-Lyases
references.citation: J Biol Chem. 2001 Jun 1;276(22):19190-6
references.pmid: 11279129
references.citation: Nucleic Acids Res. 2010 Jul;38(Web Server issue):W545-9
references.pmid: 20457744
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21
references.pmid: 20057044
references.citation: J Mol Biol. 2003 Mar 14;327(1):193-202
references.pmid: 12614618
references.citation: Arch Biochem Biophys. 2007 Nov 15;467(2):144-53
references.pmid: 17889824
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
references.pmid: 20383002
references.citation: Nucleic Acids Res. 2010 Jul;38(Web Server issue):W529-33
references.pmid: 20478830
references.citation: Protein Sci. 2004 Nov;13(11):3006-16
references.pmid: 15459342
references.citation: J Bacteriol. 1980 Aug;143(2):644-51
references.pmid: 7009558
references.citation: Biochemistry. 1985 Dec 3;24(25):7178-82
references.pmid: 4084574
references.citation: Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1414-21
references.pmid: 12876343
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):355-67
references.pmid: 21460454
references.citation: J Biol Chem. 2000 Oct 13;275(41):31838-46
references.pmid: 10922366
references.citation: Protein Expr Purif. 2008 Apr;58(2):210-21
references.pmid: 18171622
references.citation: Angew Chem Int Ed Engl. 2010 Mar 22;49(13):2324-7
references.pmid: 20187055
references.citation: EMBO J. 2000 Dec 1;19(23):6299-310
references.pmid: 11101502
references.citation: Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):14339-44
references.pmid: 14617778
references.citation: Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1762-6
references.pmid: 14501115
references.citation: J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
references.pmid: 19461840
references.citation: J Biosci Bioeng. 2010 Jun;109(6):564-9
references.pmid: 20471595