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Godoi, PH, Galhardo, RS, Luche, DD, Van Sluys, MA, Menck, CF and Oliva, G (2006) Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana. J. Biol. Chem. 281:30957-66


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.


PubMed Online version:10.1074/jbc.M604469200


Adenosine Triphosphate/chemistry; Amino Acid Sequence; Arabidopsis/enzymology; Arabidopsis Proteins/chemistry; Arabidopsis Proteins/metabolism; Binding Sites; Escherichia coli/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Thiamine Pyrophosphate/chemistry; Thiazoles/chemistry



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