3EOE

Crystal Structure of Pyruvate Kinase from toxoplasma gondii, 55.m00007

Summary for 3EOE

• Entry DOI: 10.2210/pdb3eoe/pdb
• Descriptor: Pyruvate kinase, GLYCEROL (3 entities in total)
• Functional Keywords: malaria kinase pyruvate structural genomics, glycolysis, magnesium, metal-binding, transferase, structural genomics consortium, sgc
• Biological source: Toxoplasma gondii
• Total number of polymer chains: 4
• Total formula weight: 223993.85

Authors

Wernimont, A.K.,Lew, J.,Kozieradzki, I.,Wasney, G.,Hassani, A.,Vedadi, M.,Cossar, D.,Schapiro, M.,Bochkarev, A.,Arrowsmith, C.H.,Bountra, C.,Weigelt, J.,Edwards, A.M.,Hui, R.,Pizarro, J.,Structural Genomics Consortium (SGC) (deposition date: 2008-09-26, release date: 2008-10-14, Last modification date: 2024-02-21)

Primary citation

Bakszt, R.,Wernimont, A.,Allali-Hassani, A.,Mok, M.W.,Hills, T.,Hui, R.,Pizarro, J.C.
The crystal structure of Toxoplasma gondii pyruvate kinase 1.
Plos One, 5:e12736-e12736, 2010

PubMed Abstract: Pyruvate kinase (PK), which catalyzes the final step in glycolysis converting phosphoenolpyruvate to pyruvate, is a central metabolic regulator in most organisms. Consequently PK represents an attractive therapeutic target in cancer and human pathogens, like Apicomplexans. The phylum Aplicomplexa, a group of exclusively parasitic organisms, includes the genera Plasmodium, Cryptosporidium and Toxoplasma, the etiological agents of malaria, cryptosporidiosis and toxoplasmosis respectively. Toxoplasma gondii infection causes a mild illness and is a very common infection affecting nearly one third of the world's population.

PubMed: 20856875
DOI: 10.1371/journal.pone.0012736

Experimental method

X-RAY DIFFRACTION (2.31 Å)