7z4m | pdb_00007z4m

Plasmodium falciparum pyruvate kinase complexed with Mg2+ and K+

spinqualitylabelsall models 7z4m, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7z4m is a 1 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, K, MG, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [C6KTA4_PLAF7] Publication Abstract from PubMed The protozoan parasite Plasmodium falciparum causes the most severe form of malaria and is highly dependent on glycolysis. Glycolytic enzymes were shown to be massively redox regulated, inter alia via oxidative post-translational modifications (oxPTMs) of their cysteine residues. In this study, we identified P. falciparum pyruvate kinase (PfPK) C49 and C343 as amino acid residues essentially involved in maintaining structural and functional integrity of the enzyme. The mutation of these cysteines resulted in an altered substrate affinity, lower enzymatic activities, and, as studied by X-ray crystallography, conformational changes within the A-domain where the substrate binding site is located. Although the loss of a cysteine evoked an impaired catalysis in both mutants, the effects observed for mutant C49A were more severe: multiple conformational changes, caused by the loss of two hydrogen bonds, impeded proper substrate binding and thus the transfer of phosphate upon catalysis. Prominent role of cysteine residues C49 and C343 in regulating Plasmodiumfalciparum pyruvate kinase activity.,Dillenberger M, Rahlfs S, Becker K, Fritz-Wolf K Structure. 2022 Aug 17. pii: S0969-2126(22)00316-1. doi:, 10.1016/j.str.2022.08.001. PMID:35998635 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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