2tps
From Proteopedia
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| , resolution 1.25Å | |||||||
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| Ligands: | , , | ||||||
| Activity: | Thiamine-phosphate diphosphorylase, with EC number 2.5.1.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 05:04:05 2008
