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2.4.2.60: cysteine-dependent adenosine diphosphate thiazole synthase

This is an abbreviated version!
For detailed information about cysteine-dependent adenosine diphosphate thiazole synthase, go to the full flat file.

Reaction

NAD+
+
glycine
 +
[ADP-thiazole synthase]-L-cysteine
=
nicotinamide
 +
ADP-5-ethyl-4-methylthiazole-2-carboxylate
 +
[ADP-thiazole synthase]-dehydroalanine
 + 3 H2O

Synonyms

ADP-thiazole synthase, CyPBP37, NCU06110, Thi-4, THI1, Thi4

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.60 cysteine-dependent adenosine diphosphate thiazole synthase

Crystallization

Crystallization on EC 2.4.2.60 - cysteine-dependent adenosine diphosphate thiazole synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.6 A resolution, enzyme contains bound 2-carboxylate-4-methyl-5-beta-(ethyl adenosine 5'-diphosphate) thiazole
structure with bound glycine imine intermediate and iron. The Thi4 orthologs from Methanocaldococcus jannaschii and Methanocaldococcus igneus are structurally similar to Thi4 from Saccharomyces cerevisiae. All active site residues are conserved except for a key cysteine residue, which in Saccharomyces cerevisiae is the source of the thiazole sulfur atom
Methanocaldococcus igneus
-
structure in complex with ADP-ribulose. The Thi4 orthologs from Methanocaldococcus jannaschii and Methanocaldococcus igneus are structurally similar to Thi4 from Saccharomyces cerevisiae. All active site residues are conserved except for a key cysteine residue, which in Saccharomyces cerevisiae is the source of the thiazole sulfur atom
C205S variant with a bound glycine imine intermediate, hanging drop vapor diffusion method, using 25% (w/v) PEG1500, 0.0125 M succinic acid, 0.044 M sodium dihydrogen phosphate, and 0.044 M glycine, pH 8.5
structure of mutant C205S with a bound glycine imine intermediate. Comparison with structures of Methanococcus jannaschii and Methanococcus igneus homologues
to 1.8 A resolution. Thi4 exists as an octamer with two monomers in the asymmetric unit. A tightly bound adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid is present at the active site. The Thi4 structure reveals a protein structure with a GR2 domain that binds NAD instead of FAD