%0 Journal Article %1 Tripathi.2007 %A Tripathi, Timir %A Rahlfs, Stefan %A Becker, Katja %A Bhakuni, Vinod %D 2007 %J BMC Struct Biol %K Animals Biopolymers Dimerization Electrophoresis Glutathione Glutathione_Transferase IFZ Plasmodium_falciparum Polyacrylamide_Gel Protein_Conformation Protein_Denaturation Recombinant_Proteins %P 67-67 %T Glutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase %V 7 %X BACKGROUND: In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one typical glutathione S-transferase. This enzyme, PfGST, cannot be assigned to any of the known GST classes and represents a most interesting target for antimalarial drug development. The PfGST under native conditions forms non-covalently linked higher aggregates with major population (approximately 98%) being tetramer. However, in the presence of 2 mM GSH, a dimer of PfGST is observed. Recently reported study on binding and catalytic properties of PfGST indicated a GSH dependent low-high affinity transition with simultaneous binding of two GSH molecules to PfGST dimer suggesting that GSH binds to low affinity inactive enzyme dimer converting it to high affinity functionally active dimer. In order to understand the role of GSH in tetramer-dimer transition of PfGST as well as in modulation of functional activity of the enzyme, detailed structural, functional and stability studie

@article{Tripathi.2007, abstract = {BACKGROUND: In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one typical glutathione S-transferase. This enzyme, PfGST, cannot be assigned to any of the known GST classes and represents a most interesting target for antimalarial drug development. The PfGST under native conditions forms non-covalently linked higher aggregates with major population (approximately 98%) being tetramer. However, in the presence of 2 mM GSH, a dimer of PfGST is observed. Recently reported study on binding and catalytic properties of PfGST indicated a GSH dependent low-high affinity transition with simultaneous binding of two GSH molecules to PfGST dimer suggesting that GSH binds to low affinity inactive enzyme dimer converting it to high affinity functionally active dimer. In order to understand the role of GSH in tetramer-dimer transition of PfGST as well as in modulation of functional activity of the enzyme, detailed structural, functional and stability studie}, added-at = {2008-10-14T16:07:18.000+0200}, author = {Tripathi, Timir and Rahlfs, Stefan and Becker, Katja and Bhakuni, Vinod}, biburl = {https://www.bibsonomy.org/bibtex/2e50b48ede2d548f29c9be36590f6947a/nutribiochem}, interhash = {f677b27e4c9526aa511fc2989c3da8f8}, intrahash = {e50b48ede2d548f29c9be36590f6947a}, issn = {1472-6807}, journal = {BMC Struct Biol}, keywords = {Animals Biopolymers Dimerization Electrophoresis Glutathione Glutathione_Transferase IFZ Plasmodium_falciparum Polyacrylamide_Gel Protein_Conformation Protein_Denaturation Recombinant_Proteins}, pages = {67-67}, timestamp = {2008-10-14T16:08:42.000+0200}, title = {Glutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase}, volume = 7, year = 2007 }