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http://purl.uniprot.org/citations/16912043http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16912043http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16912043http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/16912043http://www.w3.org/2000/01/rdf-schema#comment"Thiamin pyrophosphate is an essential coenzyme in all organisms that depend on fermentation, respiration or photosynthesis to produce ATP. It is synthesized through two independent biosynthetic routes: one for the synthesis of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate (pyrimidine moiety) and another for the synthesis of 4-methyl-5-(beta-hydroxyethyl) thiazole phosphate (thiazole moiety). Herein, we will describe the three-dimensional structure of THI1 protein from Arabidopsis thaliana determined by single wavelength anomalous diffraction to 1.6A resolution. The protein was produced using heterologous expression in bacteria, unexpectedly bound to 2-carboxylate-4-methyl-5-beta-(ethyl adenosine 5-diphosphate) thiazole, a potential intermediate of the thiazole biosynthesis in Eukaryotes. THI1 has a topology similar to dinucleotide binding domains and although details concerning its function are unknown, this work provides new clues about the thiazole biosynthesis in Eukaryotes."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m604469200"xsd:string
http://purl.uniprot.org/citations/16912043http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m604469200"xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Menck C.F."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Menck C.F."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Van Sluys M.A."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Van Sluys M.A."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Oliva G."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Oliva G."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Galhardo R.S."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Galhardo R.S."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Godoi P.H."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Godoi P.H."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Luche D.D."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/author"Luche D.D."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/pages"30957-30966"xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/pages"30957-30966"xsd:string
http://purl.uniprot.org/citations/16912043http://purl.uniprot.org/core/title"Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana."xsd:string