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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...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2006
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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. |
format | Text |
id | pubmed-1616948 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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