1RP0

Crystal Structure of Thi1 protein from Arabidopsis thaliana

Summary for 1RP0

• Entry DOI: 10.2210/pdb1rp0/pdb
• Descriptor: Thiazole biosynthetic enzyme, ZINC ION, ADENOSINE DIPHOSPHATE 5-(BETA-ETHYL)-4-METHYL-THIAZOLE-2-CARBOXYLIC ACID, ... (5 entities in total)
• Functional Keywords: protein ligand complex, biosynthetic protein
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Plastid, chloroplast membrane; Peripheral membrane protein: Q38814
• Total number of polymer chains: 2
• Total formula weight: 61625.11

Authors

Godoi, P.H.C.,Van Sluys, M.A.,Menck, C.F.M.,Oliva, G. (deposition date: 2003-12-02, release date: 2005-02-22, Last modification date: 2024-02-14)

Primary citation

Godoi, P.H.,Galhardo, R.S.,Luche, D.D.,Van Sluys, M.A.,Menck, C.F.,Oliva, G.
Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana.
J.Biol.Chem., 281:30957-30966, 2006

PubMed 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.

PubMed: 16912043
DOI: 10.1074/jbc.M604469200

Experimental method

X-RAY DIFFRACTION (1.6 Å)