4H6D

Crystal structure of PLP-soaked HMP synthase Thi5 from S. cerevisiae

4H6D の概要

• エントリーDOI: 10.2210/pdb4h6d/pdb
• 関連するPDBエントリー: 4H65 4H67
• 分子名称: Pyrimidine precursor biosynthesis enzyme THI5, PYRIDOXAL-5'-PHOSPHATE (2 entities in total)
• 機能のキーワード: synthase, transferase
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 316313.26

構造登録者

Coquille, S.C.,Roux, C.,Fitzpatrick, T.,Thore, S. (登録日: 2012-09-19, 公開日: 2012-10-17, 最終更新日: 2023-09-20)

主引用文献

Coquille, S.,Roux, C.,Fitzpatrick, T.B.,Thore, S.
The Last Piece in the Vitamin B1 Biosynthesis Puzzle: STRUCTURAL AND FUNCTIONAL INSIGHT INTO YEAST 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE (HMP-P) SYNTHASE.
J.Biol.Chem., 287:42333-42343, 2012

PubMed Abstract: Vitamin B(1) is essential for all organisms being well recognized as a necessary cofactor for key metabolic pathways such as glycolysis, and was more recently implicated in DNA damage responses. Little is known about the enzyme responsible for the formation of the pyrimidine moiety (4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase). We report a structure-function study of the HMP-P synthase from yeast, THI5p. Our crystallographic structure shows that THI5p is a mix between periplasmic binding proteins and pyridoxal 5'-phosphate-dependent enzymes. Mutational and yeast complementation studies identify the key residues for HMP-P biosynthesis as well as the use of pyridoxal 5'-phosphate as a substrate rather than as a cofactor. Furthermore, we could show that iron binding to HMP-P synthase is essential for the reaction.

PubMed: 23048037
DOI: 10.1074/jbc.M112.397240

実験手法

X-RAY DIFFRACTION (2.9 Å)