Dependence of the mechanical intersubunit communication of a dimeric protein to specific mutation as revealed by molecular dynamics simulation
✍ Scribed by M. Falconi; F. Venerini; A. Desideri
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 510 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0167-7322
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✦ Synopsis
Analysis of 300 ps of molecular dynamics simulation carried out on the wild type and on a Xenopus laevis Cu,Zn superoxide dismutase mutant indicates that the two proteins display a distinct dynnmical behaviour.
In both cases time evolution of the Voronoi volumes of the single subunits indicate that one monomer shows higher volume fluctuations and a more variable behaviour if compared to the other one. The dynamical structural asymmetry is higher in the mutant than in the wild type enzyme. Dynamical correlation of the Voronoi volume of one subunit with that of the other shows that in the mutant changes in volume of one subunit are transmitted to the other subunit more slowly than in the native enzyme. This result indicate that perturbation of the mechanical comm~mication between the two subunits may be brought about by mutations located in the active sites, far from the intersubunit interface of the enzyme, suggesting a strict interrelation even between protein regions located far away.