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dc.contributor.authorDillenberger, Melissa
dc.contributor.authorWerner, Anke-Dorothee
dc.contributor.authorVelten, Ann-Sophie
dc.contributor.authorRahlfs, Stefan
dc.contributor.authorBecker, Katja
dc.contributor.authorFritz-Wolf, Karin
dc.date.accessioned2024-02-07T14:30:00Z
dc.date.available2024-02-07T14:30:00Z
dc.date.issued2023
dc.identifier.urihttps://jlupub.ub.uni-giessen.de//handle/jlupub/18992
dc.identifier.urihttp://dx.doi.org/10.22029/jlupub-18353
dc.description.abstractThe protozoan parasite Plasmodium falciparum is the causative pathogen of the most severe form of malaria, for which novel strategies for treatment are urgently required. The primary energy supply for intraerythrocytic stages of Plasmodium is the production of ATP via glycolysis. Due to the parasite’s strong dependence on this pathway and the significant structural differences of its glycolytic enzymes compared to its human counterpart, glycolysis is considered a potential drug target. In this study, we provide the first three-dimensional protein structure of P. falciparum hexokinase (PfHK) containing novel information about the mechanisms of PfHK. We identified for the first time a Plasmodium-specific insertion that lines the active site. Moreover, we propose that this insertion plays a role in ATP binding. Residues of the insertion further seem to affect the tetrameric interface and therefore suggest a special way of communication among the different monomers. In addition, we confirmed that PfHK is targeted and affected by oxidative posttranslational modifications (oxPTMs). Both S-glutathionylation and S-nitrosation revealed an inhibitory effect on the enzymatic activity of PfHK.
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (DFG); ROR-ID:018mejw64
dc.language.isoen
dc.rightsNamensnennung 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subject.ddcddc:640
dc.subject.ddcddc:360
dc.titleStructural Analysis of Plasmodium falciparum Hexokinase Provides Novel Information about Catalysis Due to a Plasmodium-Specific Insertion
dc.typearticle
local.affiliationFB 09 - Agrarwissenschaften, Ökotrophologie und Umweltmanagement
local.projectGrant BE1540/23-2 within the DFG Priority Program 1710 on Thiol Switches
local.source.spage1
local.source.epage20
local.source.journaltitleInternational journal of molecular sciences
local.source.volume24
local.source.articlenumber12739
local.source.urihttps://doi.org/10.3390/ijms241612739


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