3GG8
Crystal structure of the Toxoplasma gondii Pyruvate Kinase N terminal truncated
Summary for 3GG8
Entry DOI | 10.2210/pdb3gg8/pdb |
Descriptor | Pyruvate kinase, SULFATE ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | malaria, pyruvate kinase, genomics, proteomics, glycolysis, kinase, magnesium, pyruvate, transferase, structural genomics, structural genomics consortium, sgc |
Biological source | Toxoplasma gondii |
Total number of polymer chains | 4 |
Total formula weight | 224001.78 |
Authors | Wernimont, A.K.,Lew, J.,Allali-Hassani, A.,Vedadi, M.,Bochkarev, A.,Arrowsmith, C.H.,Bountra, C.,Weigelt, J.,Edwards, A.M.,Hills, T.,Schapira, M.,Hui, R.,Pizarro, J.C.,Structural Genomics Consortium (SGC) (deposition date: 2009-02-27, release date: 2009-05-26, Last modification date: 2023-09-06) |
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 Cited by 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: 20856875DOI: 10.1371/journal.pone.0012736 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
Download full validation report