6SU2

Trypanosoma congolense pyruvate kinase in complex with citrate and glycerol

6SU2 の概要

• エントリーDOI: 10.2210/pdb6su2/pdb
• 分子名称: Pyruvate kinase, 1,6-di-O-phosphono-beta-D-fructofuranose, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: pyruvate kinase, complex, glycolysis, trypanosomes, transferase
• 由来する生物種: Trypanosoma congolense IL3000
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 227154.90

構造登録者

Sterckx, Y.G.-J.,Pinto Torres, J.E. (登録日: 2019-09-12, 公開日: 2020-03-04, 最終更新日: 2024-05-15)

主引用文献

Pinto Torres, J.E.,Yuan, M.,Goossens, J.,Versees, W.,Caljon, G.,Michels, P.A.,Walkinshaw, M.D.,Magez, S.,Sterckx, Y.G.
Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase.
Mol.Biochem.Parasitol., 236:111263-111263, 2020

PubMed Abstract: Trypanosoma are blood-borne parasites and are the causative agents of neglected tropical diseases (NTDs) affecting both humans and animals. These parasites mainly rely on glycolysis for their energy production within the mammalian host, which is why trypanosomal glycolytic enzymes have been pursued as interesting targets for the development of trypanocidal drugs. The structure-function relationships of pyruvate kinases (PYKs) from trypanosomatids (Trypanosoma and Leishmania) have been well-studied within this context. In this paper, we describe the structural and enzymatic characterization of PYK from T. congolense (TcoPYK), the main causative agent of Animal African Trypanosomosis (AAT), by employing a combination of enzymatic assays, thermal unfolding studies and X-ray crystallography.

PubMed: 32084384
DOI: 10.1016/j.molbiopara.2020.111263

実験手法

X-RAY DIFFRACTION (3 Å)