6SU1

Trypanosoma congolense pyruvate kinase in complex with citrate and glycerol

Summary for 6SU1

• Entry DOI: 10.2210/pdb6su1/pdb
• Descriptor: Pyruvate kinase, GLYCEROL, CITRIC ACID, ... (6 entities in total)
• Functional Keywords: pyruvate kinase, complex, glycolysis, trypanosomes, transferase
• Biological source: Trypanosoma congolense IL3000
• Total number of polymer chains: 8
• Total formula weight: 453724.42

Authors

Sterckx, Y.G.-J.,Pinto Torres, J.E. (deposition date: 2019-09-12, release date: 2020-03-04, Last modification date: 2024-01-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3 Å)