Literature summary for 2.8.1.10 extracted from

Settembre, E.C.; Dorrestein, P.C.; Zhai, H.; Chatterjee, A.; McLafferty, F.W.; Begley, T.P.; Ealick, S.E.
Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex (2004), Biochemistry, 43, 11647-11657.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of ThiG in complex with ThiS, the sulfur carrier protein, at 3.15 A resolution. Thiazole synthase is a tetramer with 222 symmetry. The monomer is a (betaalpha)8 barrel with similarities to the aldolase class 1 and flavin mononucleotide dependent oxidoreductase and phosphate binding superfamilies. The sulfur carrier protein ThiS is a compact protein with a fold similar to that of ubiquitin. Modeling the substrate, deoxy-D-xylulose 5-phosphate in the active site identifies Glu98 and Asp182 as active site residues likely to be involved in the catalysis of thiazole formation	Bacillus subtilis

Crystallization (Comment)

Organism

structure of ThiG in complex with ThiS, the sulfur carrier protein, at 3.15 A resolution. Thiazole synthase is a tetramer with 222 symmetry. The monomer is a (betaalpha)8 barrel with similarities to the aldolase class 1 and flavin mononucleotide dependent oxidoreductase and phosphate binding superfamilies. The sulfur carrier protein ThiS is a compact protein with a fold similar to that of ubiquitin. Modeling the substrate, deoxy-D-xylulose 5-phosphate in the active site identifies Glu98 and Asp182 as active site residues likely to be involved in the catalysis of thiazole formation

Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
D182A	no residual activity	Bacillus subtilis
E98A	less than 3% residual activity	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O31618	-	-

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Release 2023.1 (January 2023)