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6su1

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Trypanosoma congolense pyruvate kinase in complex with citrate and glycerol

Structural highlights

6su1 is a 8 chain structure with sequence from Trypanosoma congolense IL3000. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G0UYF4_TRYCI

Publication Abstract from PubMed

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.

Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase.,Pinto Torres JE, Yuan M, Goossens J, Versees W, Caljon G, Michels PA, Walkinshaw MD, Magez S, Sterckx YG Mol Biochem Parasitol. 2020 Feb 19;236:111263. doi:, 10.1016/j.molbiopara.2020.111263. PMID:32084384^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pinto Torres JE, Yuan M, Goossens J, Versees W, Caljon G, Michels PA, Walkinshaw MD, Magez S, Sterckx YG. Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase. Mol Biochem Parasitol. 2020 Feb 19;236:111263. doi:, 10.1016/j.molbiopara.2020.111263. PMID:32084384 doi:http://dx.doi.org/10.1016/j.molbiopara.2020.111263