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http://purl.uniprot.org/citations/15459342http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15459342http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15459342http://www.w3.org/2000/01/rdf-schema#comment"The crystal structure of the flavoprotein Pad1 from Escherichia coli O157:H7 complexed with the cofactor FMN has been determined by the multiple anomalous diffraction method and refined at 2.0 A resolution. This protein is a paralog of UbiX (3-octaprenyl-4-hydroxybenzoate carboxylyase, 51% sequence identity) that catalyzes the third step in ubiquinone biosynthesis and to Saccharomyces cerevisiae Pad1 (54% identity), an enzyme that confers resistance to the antimicrobial compounds phenylacrylic acids through decarboxylation of these compounds. Each Pad1 monomer consists of a typical Rossmann fold containing a non-covalently bound molecule of FMN. The fold of Pad1 is similar to MrsD, an enzyme associated with lantibiotic synthesis; EpiD, a peptidyl-cysteine decarboxylase; and AtHAL3a, the enzyme, which decarboxylates 4'-phosphopantothenoylcysteine to 4'-phosphopantetheine during coenzyme A biosynthesis, all with a similar location of the FMN binding site at the interface between two monomers, yet each having little sequence similarity to one another. All of these proteins associate into oligomers, with a trimer forming the common structural unit in each case. In MrsD and EpiD, which belong to the homo-dodecameric flavin-containing cysteine decarboxylase (HFCD) family, these trimers associate further into dodecamers. Pad1 also forms dodecamers, although the association of the trimers is completely different, resulting in exposure of a different side of the trimer unit to the solvent. This exposure affects the location of the substrate binding site and, specifically, its access to the FMN cofactor. Therefore, Pad1 forms a separate family, distinguishable from the HFCD family."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.org/dc/terms/identifier"doi:10.1110/ps.04953004"xsd:string
http://purl.uniprot.org/citations/15459342http://purl.org/dc/terms/identifier"doi:10.1110/ps.04953004"xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Cygler M."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Cygler M."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Hung L.-W."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Hung L.-W."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Matte A."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Matte A."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Tocilj A."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Tocilj A."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Rangarajan E.S."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Rangarajan E.S."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Iannuzzi P."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/author"Iannuzzi P."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/pages"3006-3016"xsd:string
http://purl.uniprot.org/citations/15459342http://purl.uniprot.org/core/pages"3006-3016"xsd:string