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J. Biol. Chem., Vol. 281, Issue 41, 30957-30966, October 13, 2006

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Structure of the Thiazole Biosynthetic Enzyme THI1 from Arabidopsis thaliana^*

Paulo H. C. Godoi¹, Rodrigo S. Galhardo^¶, Douglas D. Luche^¶, Marie-Anne Van Sluys^||, Carlos F. M. Menck^¶, and Glaucius Oliva²

From the Departamento de Física e Informática, Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, SP, CP 369, 13560-970, Brazil, the Departamento de Físico-Química, Instituto de Química de São Carlos, Universidade de São Paulo, São Carlos, SP, 13560-970, Brazil, the ^||Departamento de Botânica, Instituto de Biociências, Universidade de São Paulo, São Paulo, SP, 05508-900, Brazil, and the ^¶Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, SP, 05508-900, Brazil

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-(-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 1.6Å resolution. The protein was produced using heterologous expression in bacteria, unexpectedly bound to 2-carboxylate-4-methyl-5--(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.

Received for publication, May 10, 2006 , and in revised form, August 11, 2006.

The atomic coordinates and structure factors (code 1RP0) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by FAPESP (São Paulo, Brazil) and CNPq (Brasília, Brazil). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables 1 and 2 and Figs. 1 and 2.

¹ Current address: Burnham Inst. for Medical Research, La Jolla, CA 92037.

² To whom correspondence should be addressed. E-mail: oliva{at}if.sc.usp.br.

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