Functionally important correlated motions in the single-stranded DNA-binding protein encoded by filamentous phage Pf3.
J Mol Biol
; 287(3): 569-77, 1999 Apr 02.
Article
em En
| MEDLINE
| ID: mdl-10092460
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Virais
/
Inovirus
/
Proteínas de Ligação a DNA
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Holanda