Nucleic Acids Research Advance Access originally published online on August 25, 2006
Nucleic Acids Research 2006 34(15):4160-4167; doi:10.1093/nar/gkl540
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Nucleic Acids Research, 2006, Vol. 34, No. 15 4160-4167
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Snf2 family ATPases and DExx box helicases: differences and unifying concepts from high-resolution crystal structures
1 Gene Center, University of Munich Feodor-Lynen-Strasse 25, D-81377 Munich, Germany 2 Department of Chemistry and Biochemistry, University of Munich Feodor-Lynen-Strasse 25, D-81377 Munich, Germany 3 Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee Dundee DD1 5EH, UK
*To whom correspondence should be addressed. Tel: +49 89 218076953; Fax: +49 89 218076999; Email: hopfner{at}lmb.uni-muenchen.de
*Correspondence may also be addressed to: Tom Owen-Hughes.Tel: +44 1382 385796; Fax: +44 1382 388072; Email: t.a.owenhughes{at}dundee.ac.uk
Received March 27, 2006. Revised July 12, 2006. Accepted July 13, 2006.
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.
Present address: Andrew Flaus, Department of Biochemistry, National University of Ireland Galway, Ireland
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