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Functionally important correlated motions in the single-stranded DNA-binding protein encoded by filamentous phage Pf3.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Horstink LM,Abseher R,Nilges M,Hilbers CW

doi

10.1006/jmbi.1999.2629

keywords:

subject

Has Abstract

pub_date

1999-04-02 00:00:00

pages

569-77

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)92629-3

journal_volume

287

pub_type

杂志文章

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