2tps

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Template:STRUCTURE 2tps

THIAMIN PHOSPHATE SYNTHASE


Overview

The characterization of a three-gene operon (the thiC operon) at 331 min, which is involved in thiamine biosynthesis in Bacillus subtilis, is described. The first gene in the operon is homologous to transcription activators in the lysR family. The second and third genes (thiK and thiC) have been subcloned and overexpressed in Escherichia coli. ThiK (30 kDa) catalyzes the phosphorylation of 4-methyl-5-(beta-hydroxyethyl)thiazole. ThiC (27 kDa) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate by 4-methyl-5-(beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. Transcription of the thiC operon is not regulated by thiamine or 2-methyl-4-amino-5-hydroxymethylpyrimidine and is only slightly repressed by 4-methyl-5-(beta-hydroxyethyl)thiazole.

About this Structure

2TPS is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis., Zhang Y, Taylor SV, Chiu HJ, Begley TP, J Bacteriol. 1997 May;179(9):3030-5. PMID:9139923 Page seeded by OCA on Sun May 4 17:25:51 2008

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