| Author(s): |
Godoi, Paulo H. C.
;
Galhardo, Rodrigo S.
;
Luche, Douglas D.
;
Van Sluys, Marie-Anne
;
Menck, Carlos F. M.
[5]
;
Oliva, Glaucius
Total Authors: 6
|
| Document type: | Journal article |
| Source: | Journal of Biological Chemistry; v. 281, n. 41, p. 30957-30966, Oct. 2006. |
| Field of knowledge: | Biological Sciences - Biochemistry |
| Abstract | |
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. (AU) | |
| FAPESP's process: | 03/13255-5 - DNA repair genes: functional analysis and evolution |
| Grantee: | Carlos Frederico Martins Menck |
| Support type: | Research Projects - Thematic Grants |