6C07

Crystal Structure of S-Adenosylmethionine synthetase (MetK/Mat) from Cryptosporidium parvum

6C07 の概要

• エントリーDOI: 10.2210/pdb6c07/pdb
• 分子名称: S-adenosylmethionine synthase, CHLORIDE ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: s-adenosylmethionine synthetase, enzyme metabolism, anti-infective target, anti-cancer target, transferase
• 由来する生物種: Cryptosporidium parvum (strain Iowa II)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 179864.26

構造登録者

Ohren, J.F.,Viola, R.E. (登録日: 2017-12-28, 公開日: 2019-01-16, 最終更新日: 2023-10-04)

主引用文献

Ohren, J.,Parungao, G.G.,Viola, R.E.
Structure of a critical metabolic enzyme: S-adenosylmethionine synthetase from Cryptosporidium parvum.
Acta Crystallogr F Struct Biol Commun, 75:290-298, 2019

PubMed Abstract: S-Adenosyl-L-methionine (AdoMet), the primary methyl donor in most biological methylation reactions, is produced from ATP and methionine in a multistep reaction catalyzed by AdoMet synthetase. The diversity of group-transfer reactions that involve AdoMet places this compound at a key crossroads in amino-acid, nucleic acid and lipid metabolism, and disruption of its synthesis has adverse consequences for all forms of life. The family of AdoMet synthetases is highly conserved, and structures of this enzyme have been determined from organisms ranging from bacteria to humans. Here, the structure of an AdoMet synthetase from the infectious parasite Cryptosporidium parvum has been determined as part of an effort to identify structural differences in this enzyme family that can guide the development of species-selective inhibitors. This enzyme form has a less extensive subunit interface than some previously determined structures, and contains some key structural differences from the human enzyme in an allosteric site, presenting an opportunity for the design of selective inhibitors against the AdoMet synthetase from this organism.

PubMed: 30950830
DOI: 10.1107/S2053230X19002772

実験手法

X-RAY DIFFRACTION (1.85 Å)