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>