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dc.contributor.authorBerneburg, Isabell
dc.contributor.authorRahlfs, Stefan
dc.contributor.authorBecker, Katja
dc.contributor.authorFritz-Wolf, Karin
dc.date.accessioned2023-04-13T12:37:24Z
dc.date.available2023-04-13T12:37:24Z
dc.date.issued2022
dc.identifier.urihttps://jlupub.ub.uni-giessen.de//handle/jlupub/16209
dc.identifier.urihttp://dx.doi.org/10.22029/jlupub-15591
dc.description.abstractSince unicellular parasites highly depend on NADPH as a source for reducing equivalents, the pentose phosphate pathway, especially the first and rate-limiting NADPH-producing enzyme glucose 6-phosphate dehydrogenase (G6PD), is considered an excellent antitrypanosomatid drug target. Here we present the crystal structure of Leishmania donovani G6PD (LdG6PD) elucidating the unique N-terminal domain of Kinetoplastida G6PDs. Our investigations on the function of the N-domain suggest its involvement in the formation of a tetramer that is completely different from related Trypanosoma G6PDs. Structural and functional investigations further provide interesting insights into the binding mode of LdG6PD, following an ordered mechanism, which is confirmed by a G6P-induced domain shift and rotation of the helical N-domain. Taken together, these insights into LdG6PD contribute to the understanding of G6PDs’ molecular mechanisms and provide an excellent basis for further drug discovery approaches.
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.titleCrystal structure of Leishmania donovani glucose 6-phosphate dehydrogenase reveals a unique N-terminal domain
dc.typearticle
local.affiliationFB 09 - Agrarwissenschaften, Ökotrophologie und Umweltmanagement
local.source.spage1
local.source.epage14
local.source.journaltitleCommunications biology
local.source.volume5
local.source.articlenumber1353
local.source.urihttps://doi.org/10.1038/s42003-022-04307-7


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