User:Wayne Decatur/Gal 4

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<Structure load='Insert PDB code or filename here' size='550' frame='true' align='right' caption='The N-terminal amino acids of Gal4p bound to DNA.' scene='70/701975/1d66_firstglance/1' />
<Structure load='Insert PDB code or filename here' size='550' frame='true' align='right' caption='The N-terminal amino acids of Gal4p bound to DNA.' scene='70/701975/1d66_firstglance/1' />
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==DNA Recognition by Gal4p==
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==Background==
Gal4p is a transcriptional activator in ''Saccharomyces cerevisiae'' that regulates the expression of genes to coordinate the response to the carbon source galactose.
Gal4p is a transcriptional activator in ''Saccharomyces cerevisiae'' that regulates the expression of genes to coordinate the response to the carbon source galactose.
Gal4p is an 881-amino-acid protein with a Zn cluster-type DNA-binding domain, a linker domain, a dimerization domain, and two acidic activation domains.
Gal4p is an 881-amino-acid protein with a Zn cluster-type DNA-binding domain, a linker domain, a dimerization domain, and two acidic activation domains.
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The structure of The protein binds as a dimer to a symmetrical 17-base-pair sequence. Specifically, the consensus Gal4-binding site is a 17-mer of sequence conforming to the motif below.<br>
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The structure of the DNA-binding domain([[1d66]]), the dimerization domain ([[1hbw]]), and the activation domain([[3bts]]) has been solved separately. There is a structure of the DNA-binding and dimerization domains as one unit as well ([[3coq]]).
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Pioneering studies on Gal4p from the Ptashne laboratory shaped our understanding of transcriptional activation in eukaryotes and Gal4p derivatives, along with the congnate promoters, have been used as tools in yeast for many years.
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==DNA Recognition by Gal4p==
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The protein binds as a dimer to a symmetrical 17-base-pair sequence. Specifically, the consensus Gal4p-binding site is a 17-mer of sequence conforming to the motif below.<br>
&nbsp;<br>
&nbsp;<br>
<span style="font-weight: bold;font-family: Courier New; font-size: 14pt">
<span style="font-weight: bold;font-family: Courier New; font-size: 14pt">
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<br>
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The DNA binding domain uses four Cys residues to coordinate the binding of Zn(II). This structure motif lets the structure accomplish more with fewer amino acids, lending an "economy of structure", specifically arranging two helices to specifically recognize a DNA binding site.
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Pioneering studies on Gal4p from the Ptashne laboratory shaped our understanding of transcriptional activation in eukaryotes and Gal4p derivatives, along with the congnate promoters, have been used as tools in yeast for many years.
 
==Reference==
==Reference==
<ref group="xtra">PMID:1557122</ref><references group="xtra"/>
<ref group="xtra">PMID:1557122</ref><references group="xtra"/>

Revision as of 16:01, 12 May 2015

Gal4p is a transcriptional activator in Saccharomyces cerevisiae that regulates the expression of genes to coordinate the response to the carbon source galactose. Structures


The N-terminal amino acids of Gal4p bound to DNA.

Drag the structure with the mouse to rotate

Background

Gal4p is a transcriptional activator in Saccharomyces cerevisiae that regulates the expression of genes to coordinate the response to the carbon source galactose. Gal4p is an 881-amino-acid protein with a Zn cluster-type DNA-binding domain, a linker domain, a dimerization domain, and two acidic activation domains. The structure of the DNA-binding domain(1d66), the dimerization domain (1hbw), and the activation domain(3bts) has been solved separately. There is a structure of the DNA-binding and dimerization domains as one unit as well (3coq).

Pioneering studies on Gal4p from the Ptashne laboratory shaped our understanding of transcriptional activation in eukaryotes and Gal4p derivatives, along with the congnate promoters, have been used as tools in yeast for many years.

DNA Recognition by Gal4p

The protein binds as a dimer to a symmetrical 17-base-pair sequence. Specifically, the consensus Gal4p-binding site is a 17-mer of sequence conforming to the motif below.
 
        5'-CGGNNNNNNNNNNNCCG-3'
           |||||||||||||||||
        3'-CGGNNNNNNNNNNNGGC-5'

The DNA binding domain uses four Cys residues to coordinate the binding of Zn(II). This structure motif lets the structure accomplish more with fewer amino acids, lending an "economy of structure", specifically arranging two helices to specifically recognize a DNA binding site.


Reference

Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur

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