10.6084/m9.figshare.2069694.v1 Ramin Ekhteiari Salmas Ramin Ekhteiari Salmas Mert Mestanoglu Mert Mestanoglu Ayhan Unlu Ayhan Unlu Mine Yurtsever Mine Yurtsever Serdar Durdagi Serdar Durdagi Mutated form (G52E) of inactive diphtheria toxin CRM197: molecular simulations clearly display effect of the mutation to NAD binding Taylor & Francis Group 2016 CRM197 MD simulations diphtheria toxin binding interactions analysis 2016-02-02 21:30:58 Journal contribution https://tandf.figshare.com/articles/journal_contribution/Mutated_form_G52E_of_inactive_diphtheria_toxin_CRM197_molecular_simulations_clearly_display_effect_of_the_mutation_to_NAD_binding/2069694 <p>Mutated 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.</p>