Insights into internal dynamics of 6-phosphogluconolactonase from Trypanosoma brucei studied by nuclear magnetic resonance and molecular dynamics
Nuclear magnetic resonance is used to investigate the backbone dynamics in 6-phosphogluconolactonase from Trypanosoma brucei (Tb6PGL) with (holo-) and without (apo-) 6-phosphogluconic acid as ligand. Relaxation data were analyzed using the model-free approach and reduced spectral density mapping. Comparison of predictions, based on 77 ns molecular dynamics simulations, with the observed relaxation rates gives insight into dynamical properties of the protein and their alteration on ligand binding. Data indicate dynamics changes in the vicinity of the binding site. More interesting is the presence of perturbations located in remote regions of this well-structured globular protein in which no large-amplitude motions are involved. This suggests that delocalized changes in dynamics that occur upon binding could be a general feature of proteintarget interactions. Proteins 2012; (c) 2011 Wiley Periodicals, Inc.
Keywords: Nmr ; relaxation ; protein dynamics ; 6-phospho-gluconolactonase (6PGL) ; molecular dynamics simulations (MD) ; Pentose-Phosphate Pathway ; Time-Scale Dynamics ; Model-Free Approach ; Nmr Relaxation ; Intrinsic Dynamics ; Protein Dynamics ; Conformational Entropy ; Backbone Dynamics ; Enzyme Catalysis ; Binding
Record created on 2012-04-12, modified on 2016-08-09