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Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures

Proteins with sequence similarity to the yeast Snf2 protein form a large family of ATPases that act to alter the structure of a diverse range of DNA–protein structures including chromatin. Snf2 family enzymes are related in sequence to DExx box helicases, yet they do not possess helicase activity. R...

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Detalles Bibliográficos
Autores principales: Dürr, Harald, Flaus, Andrew, Owen-Hughes, Tom, Hopfner, Karl-Peter
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616948/
https://www.ncbi.nlm.nih.gov/pubmed/16935875
http://dx.doi.org/10.1093/nar/gkl540
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author Dürr, Harald
Flaus, Andrew
Owen-Hughes, Tom
Hopfner, Karl-Peter
author_facet Dürr, Harald
Flaus, Andrew
Owen-Hughes, Tom
Hopfner, Karl-Peter
author_sort Dürr, Harald
collection PubMed
description Proteins with sequence similarity to the yeast Snf2 protein form a large family of ATPases that act to alter the structure of a diverse range of DNA–protein structures including chromatin. Snf2 family enzymes are related in sequence to DExx box helicases, yet they do not possess helicase activity. Recent biochemical and structural studies suggest that the mechanism by which these enzymes act involves ATP-dependent translocation on DNA. Crystal structures suggest that these enzymes travel along the minor groove, a process that can generate the torque or energy in remodelling processes. We review the recent structural and biochemical findings which suggest a common mechanistic basis underlies the action of many of both Snf2 family and DExx box helicases.
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spelling pubmed-16169482006-10-27 Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures Dürr, Harald Flaus, Andrew Owen-Hughes, Tom Hopfner, Karl-Peter Nucleic Acids Res Survey and Summary Proteins with sequence similarity to the yeast Snf2 protein form a large family of ATPases that act to alter the structure of a diverse range of DNA–protein structures including chromatin. Snf2 family enzymes are related in sequence to DExx box helicases, yet they do not possess helicase activity. Recent biochemical and structural studies suggest that the mechanism by which these enzymes act involves ATP-dependent translocation on DNA. Crystal structures suggest that these enzymes travel along the minor groove, a process that can generate the torque or energy in remodelling processes. We review the recent structural and biochemical findings which suggest a common mechanistic basis underlies the action of many of both Snf2 family and DExx box helicases. Oxford University Press 2006-09 2006-08-25 /pmc/articles/PMC1616948/ /pubmed/16935875 http://dx.doi.org/10.1093/nar/gkl540 Text en © 2006 The Author(s)
spellingShingle Survey and Summary
Dürr, Harald
Flaus, Andrew
Owen-Hughes, Tom
Hopfner, Karl-Peter
Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures
title Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures
title_full Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures
title_fullStr Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures
title_full_unstemmed Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures
title_short Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures
title_sort snf2 family atpases and dexx box helicases: differences and unifying concepts from high-resolution crystal structures
topic Survey and Summary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616948/
https://www.ncbi.nlm.nih.gov/pubmed/16935875
http://dx.doi.org/10.1093/nar/gkl540
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