The crystal structure of Toxoplasma gondii pyruvate kinase 1.

ABSTRACT:

Background

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.

Methodology/principal findings

We have determined the crystal structure of the PK1 enzyme from T. gondii, with the B domain in the open and closed

SUBMITTER: Bakszt R 

PROVIDER: S-EPMC2939071 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature