2euv
From Proteopedia
 (New page: 200px<br /><applet load="2euv" size="450" color="white" frame="true" align="right" spinBox="true"  caption="2euv, resolution 1.940Å" /> '''Principles of prote...)  | 
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| - | [[Image:2euv.gif|left|200px]]<br /><applet load="2euv" size="  | + | [[Image:2euv.gif|left|200px]]<br /><applet load="2euv" size="350" color="white" frame="true" align="right" spinBox="true"   | 
caption="2euv, resolution 1.940Å" />  | caption="2euv, resolution 1.940Å" />  | ||
'''Principles of protein-DNA recognition revealed in the structural analysis of Ndt80-MSE DNA complexes'''<br />  | '''Principles of protein-DNA recognition revealed in the structural analysis of Ndt80-MSE DNA complexes'''<br />  | ||
==Overview==  | ==Overview==  | ||
| - | The Saccharomyces cerevisiae transcription factor Ndt80 selectively binds  | + | The Saccharomyces cerevisiae transcription factor Ndt80 selectively binds a DNA consensus sequence (the middle sporulation element [MSE]) to activate gene expression after the successful completion of meiotic recombination. Here we report the X-ray crystal structures of Ndt80 bound to ten distinct MSE variants. Comparison of these structures with the structure of Ndt80 bound to a consensus MSE reveals structural principles that determine the DNA binding specificity of this transcription factor. The 5' GC-rich end of the MSE contains distinct 5'-YpG-3' steps that are recognized by arginine side chains through a combination of hydrogen bonding and cation-pi interactions. The 3' AT-rich region is recognized via minor groove contacts that sterically exclude the N2 atom of GC base pairs. The conformation of the AT-rich region is fixed by interactions with the protein that favor recognition of poly(A)-poly(T) versus mixed AT sequences through an avoidance of major groove steric clashes at 5'-ApT-3' steps.  | 
==About this Structure==  | ==About this Structure==  | ||
| - | 2EUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://  | + | 2EUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EUV OCA].   | 
==Reference==  | ==Reference==  | ||
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[[Category: Saccharomyces cerevisiae]]  | [[Category: Saccharomyces cerevisiae]]  | ||
[[Category: Single protein]]  | [[Category: Single protein]]  | ||
| - | [[Category: Glover, J  | + | [[Category: Glover, J N.]]  | 
| - | [[Category: Lamoureux, J  | + | [[Category: Lamoureux, J S.]]  | 
[[Category: beta-barrel]]  | [[Category: beta-barrel]]  | ||
[[Category: ig-fold transcription factor]]  | [[Category: ig-fold transcription factor]]  | ||
| - | ''Page seeded by [http://  | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:44 2008''  | 
Revision as of 15:14, 21 February 2008
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Principles of protein-DNA recognition revealed in the structural analysis of Ndt80-MSE DNA complexes
Overview
The Saccharomyces cerevisiae transcription factor Ndt80 selectively binds a DNA consensus sequence (the middle sporulation element [MSE]) to activate gene expression after the successful completion of meiotic recombination. Here we report the X-ray crystal structures of Ndt80 bound to ten distinct MSE variants. Comparison of these structures with the structure of Ndt80 bound to a consensus MSE reveals structural principles that determine the DNA binding specificity of this transcription factor. The 5' GC-rich end of the MSE contains distinct 5'-YpG-3' steps that are recognized by arginine side chains through a combination of hydrogen bonding and cation-pi interactions. The 3' AT-rich region is recognized via minor groove contacts that sterically exclude the N2 atom of GC base pairs. The conformation of the AT-rich region is fixed by interactions with the protein that favor recognition of poly(A)-poly(T) versus mixed AT sequences through an avoidance of major groove steric clashes at 5'-ApT-3' steps.
About this Structure
2EUV is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Principles of protein-DNA recognition revealed in the structural analysis of Ndt80-MSE DNA complexes., Lamoureux JS, Glover JN, Structure. 2006 Mar;14(3):555-65. PMID:16531239
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