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Literature summary for 2.7.1.49 extracted from

  • French, J.B.; Begley, T.P.; Ealick, S.E.
    Structure of trifunctional THI20 from yeast (2011), Acta Crystallogr. Sect. D, 67, 784-791.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.7 A resolution. Enzyme is composed of a ThiD-like N-terminal domain that catalyzes the phosphorylation of 4-amino-5-hydroxymethyl-2-methylpyrimidine and a TenA-like C-terminal domain with thiaminase activity. The structure reveals an overall dimeric organization in which N-terminal domains and C-terminal domains form ThiD-like and TenA-like local dimers. A relatively flexible linker region composed of a loop and a short helix joins the two domains. This linker region and a flexible N-terminal extension occupy the interface between the ThiD-like and TenA-like dimers. The N-terminal extension is composed of a single beta-strand that packs against and extends the length of the internal beta-sheet of the ThiD-like domain and a short alpha-helix Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q08224 bifunctional hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
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Synonyms

Synonyms Comment Organism
Thi20
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Saccharomyces cerevisiae