Publication Abstract from PubMed
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.
Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana.,Godoi PH, Galhardo RS, Luche DD, Van Sluys MA, Menck CF, Oliva G J Biol Chem. 2006 Oct 13;281(41):30957-66. Epub 2006 Aug 15. PMID:16912043[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
