Mutated form (G52E) of inactive diphtheria toxin CRM197: molecular simulations clearly display effect of the mutation to NAD binding

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dc.authoridMestanoglu, Mert/0000-0002-7984-5959
dc.authoridYurtsever, Mine/0000-0001-6504-7182
dc.authoridEkhteiari Salmas, Ramin/0000-0003-3888-5070
dc.authoridDurdagi, Serdar/0000-0002-0426-0905
dc.authoridunlu, ayhan/0000-0001-6033-7148
dc.authorwosidDurdagi, Serdar/B-6862-2009
dc.authorwosidMestanoglu, Mert/AAH-6147-2019
dc.authorwosidYurtsever, Mine/O-3748-2014
dc.authorwosidEkhteiari Salmas, Ramin/J-6401-2016
dc.authorwosidDurdagi, Serdar/J-1904-2018
dc.authorwosidunlu, ayhan/Q-1843-2016
dc.contributor.authorSalmas, Ramin Ekhteiari
dc.contributor.authorMestanoglu, Mert
dc.contributor.authorUnlu, Ayhan
dc.contributor.authorYurtsever, Mine
dc.contributor.authorDurdagi, Serdar
dc.date.accessioned2024-06-12T10:58:53Z
dc.date.available2024-06-12T10:58:53Z
dc.date.issued2016
dc.departmentTrakya Üniversitesien_US
dc.description.abstractMutated form (G52E) of diphtheria toxin (DT) CRM197 is an inactive and nontoxic enzyme. Here, we provided a molecular insight using comparative molecular dynamics (MD) simulations to clarify the influence of a single point mutation on overall protein and active-site loop. Post-processing MD analysis (i.e. stability, principal component analysis, hydrogen-bond occupancy, etc.) is carried out on both wild and mutated targets to investigate and to better understand the mechanistic differences of structural and dynamical properties on an atomic scale especially at nicotinamide adenine dinucleotide (NAD) binding site when a single mutation (G52E) happens at the DT. In addition, a docking simulation is performed for wild and mutated forms. The docking scoring analysis and docking poses results revealed that mutant form is not able to properly accommodate the NAD molecule.en_US
dc.identifier.doi10.1080/07391102.2015.1119060
dc.identifier.endpage2468en_US
dc.identifier.issn0739-1102
dc.identifier.issn1538-0254
dc.identifier.issue11en_US
dc.identifier.pmid26836774en_US
dc.identifier.scopus2-s2.0-84958538767en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage2462en_US
dc.identifier.urihttps://doi.org/10.1080/07391102.2015.1119060
dc.identifier.urihttps://hdl.handle.net/20.500.14551/20225
dc.identifier.volume34en_US
dc.identifier.wosWOS:000385577300012en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Incen_US
dc.relation.ispartofJournal Of Biomolecular Structure & Dynamicsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCRM197en_US
dc.subjectMD Simulationsen_US
dc.subjectDiphtheria Toxinen_US
dc.subjectBinding Interactions Analysisen_US
dc.subjectCrystal-Structureen_US
dc.subjectDynamicsen_US
dc.subjectStatesen_US
dc.subjectMechanismen_US
dc.subjectProteinsen_US
dc.subjectDockingen_US
dc.titleMutated form (G52E) of inactive diphtheria toxin CRM197: molecular simulations clearly display effect of the mutation to NAD bindingen_US
dc.typeArticleen_US

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