3RM5

Structure of Trifunctional THI20 from Yeast

3RM5 の概要

• エントリーDOI: 10.2210/pdb3rm5/pdb
• 分子名称: Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20, SULFATE ION (3 entities in total)
• 機能のキーワード: hmp kinase (thid), thiaminase ii, transferase
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122708.07

構造登録者

French, J.B.,Begley, T.P.,Ealick, S.E. (登録日: 2011-04-20, 公開日: 2011-09-21, 最終更新日: 2023-09-13)

主引用文献

French, J.B.,Begley, T.P.,Ealick, S.E.
Structure of trifunctional THI20 from yeast.
Acta Crystallogr.,Sect.D, 67:784-791, 2011

PubMed Abstract: In a recently characterized thiamin-salvage pathway, thiamin-degradation products are hydrolyzed by thiaminase II, yielding 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP). This compound is an intermediate in thiamin biosynthesis that, once phosphorylated by an HMP kinase, can be used to synthesize thiamin monophosphate. Here, the crystal structure of Saccharomyces cerevisiae THI20, a trifunctional enzyme containing an N-terminal HMP kinase/HMP-P kinase (ThiD-like) domain and a C-terminal thiaminase II (TenA-like) domain, is presented. Comparison to structures of the monofunctional enzymes reveals that while the ThiD-like dimer observed in THI20 resembles other ThiD structures, the TenA-like domain, which is tetrameric in all previously reported structures, forms a dimer. Similarly, the active site of the ThiD-like domain of THI20 is highly similar to other known ThiD enzymes, while the TenA-like active site shows unique features compared with previously structurally characterized TenAs. In addition, a survey of known TenA structures revealed two structural classes, both of which have distinct conserved features. The TenA domain of THI20 possesses some features of both classes, consistent with its ability to hydrolyze both thiamin and the thiamin-degradation product 2-methyl-4-amino-5-aminomethylpyrimidine.

PubMed: 21904031
DOI: 10.1107/S0907444911024814

実験手法

X-RAY DIFFRACTION (2.68 Å)