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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana

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