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3GG8

Crystal structure of the Toxoplasma gondii Pyruvate Kinase N terminal truncated

Summary for 3GG8
Entry DOI10.2210/pdb3gg8/pdb
DescriptorPyruvate kinase, SULFATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsmalaria, pyruvate kinase, genomics, proteomics, glycolysis, kinase, magnesium, pyruvate, transferase, structural genomics, structural genomics consortium, sgc
Biological sourceToxoplasma gondii
Total number of polymer chains4
Total formula weight224001.78
Authors
Primary citationBakszt, 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: 20856875
DOI: 10.1371/journal.pone.0012736
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.21 Å)
Structure validation

226707

數據於2024-10-30公開中

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