The harmonic analysis of cylindrically symmetric proteins: A comparison of Dronpa and a DNA sliding clamp

The harmonic analysis of two types of proteins with cylindrical symmetry is performed by the Standard Force Field Normal Mode Analysis and by the elastic network model. For both proteins the global elastic modes are assigned to their characteristic topologies. Dronpa is a rigid β-barrel structure, presenting the twisting, bending and breathing motion of a cylindrical rod. The β sliding clamp of Escherichia coli is a hexagonal β-wheel, consisting of rigid segments. In its spectrum four classes of vibrations are identified which are characteristic of an elastic torus. Correlation diagrams and RMSF analysis are compared. The results provide not only a comprehensive validation of the use of both methods to describe the elastic behavior according to the low-frequency normal modes, but also depict the correlated motions of β-barrel and β-wheel proteins. The harmonic flexibility of the Dronpa protein is compared to the principal components of molecular dynamics (MD) simulation. A functionally important localized cleft opening mode is found, which is not detected by harmonic analysis.

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► The harmonic properties of two proteins with cylindrical symmetry are calculated.
► The relationship between global modes and protein topology is demonstrated.
► The overlap between modes obtained by the elastic network model and by the force field normal mode analysis is calculated.
► The results are compared to a principal component analysis, based on molecular dynamics.