Document Detail


Functionally important correlated motions in the single-stranded DNA-binding protein encoded by filamentous phage Pf3.
MedLine Citation:
PMID:  10092460     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
L M Horstink; R Abseher; M Nilges; C W Hilbers
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of molecular biology     Volume:  287     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  1999 Apr 
Date Detail:
Created Date:  1999-06-07     Completed Date:  1999-06-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  569-77     Citation Subset:  IM    
Copyright Information:
Copyright 1999 Academic Press.
Affiliation:
Laboratory of Biophysical Chemistry, University of Nijmegen, Toernooiveld, Nijmegen, 6525 ED, The Netherlands.
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MeSH Terms
Descriptor/Qualifier:
DNA, Single-Stranded / metabolism
DNA, Viral / metabolism
DNA-Binding Proteins / chemistry*,  metabolism
Dimerization
Inovirus / chemistry*,  metabolism
Magnetic Resonance Spectroscopy
Models, Molecular
Protein Conformation
Thermodynamics
Viral Proteins / chemistry*,  metabolism
Chemical
Reg. No./Substance:
0/DNA, Single-Stranded; 0/DNA, Viral; 0/DNA-Binding Proteins; 0/Viral Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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