1g4d: Difference between revisions

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New page: left|200px<br /><applet load="1g4d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4d" /> '''NMR STRUCTURE OF THE MU BACTERIOPHAGE REPRES...
 
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[[Image:1g4d.gif|left|200px]]<br /><applet load="1g4d" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1g4d.gif|left|200px]]<br /><applet load="1g4d" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1g4d" />
caption="1g4d" />
'''NMR STRUCTURE OF THE MU BACTERIOPHAGE REPRESSOR DNA-BINDING DOMAIN/DNA COMPLEX'''<br />
'''NMR STRUCTURE OF THE MU BACTERIOPHAGE REPRESSOR DNA-BINDING DOMAIN/DNA COMPLEX'''<br />


==Overview==
==Overview==
We have determined the solution structure of the complex between the, 'winged-helix' enhancer binding domain of the Mu repressor protein and its, cognate DNA site. The structure reveals an unusual use for the 'wing', which becomes immobilized upon DNA binding where it makes intermolecular, hydrogen bond contacts deep within the minor groove. Although the wing is, mobile in the absence of DNA, it partially negates the large entropic, penalty associated with its burial by maintaining a small degree of, structural order in the DNA-free state. Extensive contacts are also formed, between the recognition helix and the DNA, which reads the major groove of, a highly conserved region of the binding site through a single, base-specific hydrogen bond and van der Waals contacts.
We have determined the solution structure of the complex between the 'winged-helix' enhancer binding domain of the Mu repressor protein and its cognate DNA site. The structure reveals an unusual use for the 'wing' which becomes immobilized upon DNA binding where it makes intermolecular hydrogen bond contacts deep within the minor groove. Although the wing is mobile in the absence of DNA, it partially negates the large entropic penalty associated with its burial by maintaining a small degree of structural order in the DNA-free state. Extensive contacts are also formed between the recognition helix and the DNA, which reads the major groove of a highly conserved region of the binding site through a single base-specific hydrogen bond and van der Waals contacts.


==About this Structure==
==About this Structure==
1G4D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G4D OCA].  
1G4D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4D OCA].  


==Reference==
==Reference==
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[[Category: Enterobacteria phage mu]]
[[Category: Enterobacteria phage mu]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Clubb, R.T.]]
[[Category: Clubb, R T.]]
[[Category: Iwahara, J.]]
[[Category: Iwahara, J.]]
[[Category: Wojciak, J.M.]]
[[Category: Wojciak, J M.]]
[[Category: bacteriophage mu]]
[[Category: bacteriophage mu]]
[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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[[Category: winged-helix]]
[[Category: winged-helix]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:41:40 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:57 2008''