Functionally Important Correlated Motions in the Single-stranded DNA-binding Protein Encoded by Filamentous Phage Pf3

Author： Horstink L.M. Abseher R. Nilges M. Hilbers C.W.

ISSN： 0022-2836

Source： Journal of Molecular Biology, Vol.287, Iss.3, 1999-04, pp. : 569-577

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Abstract

To elucidate the interplay between different parts of dimeric single-stranded DNA-binding proteins we have studied the correlated motions in the protein encoded by filamentous phage Pf3 via the combined use of ¹⁵N-NMR relaxation experiments, molecular dynamics simulations and essential dynamics calculations. These studies provide insight into the mechanism underlying the protein-DNA binding reaction. The most important motions can be described by a few essential modes. Most outstanding is the correlated symmetric motion of the DNA-binding wings, which are far apart in the structure. This motion determines the access of DNA to the DNA-binding domain. A correlation between the motion of the DNA-binding wing and the complex loop is indicated to play a role in the cooperative binding of the protein to DNA. These motions are in the nanosecond regime in correspondence with the ¹⁵N-NMR relaxation experiments.