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New page: left|200px<br /><applet load="1hbw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hbw" /> '''SOLUTION NMR STRUCTURE OF THE DIMERIZATION D...
 
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[[Image:1hbw.jpg|left|200px]]<br /><applet load="1hbw" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hbw.jpg|left|200px]]<br /><applet load="1hbw" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hbw" />
caption="1hbw" />
'''SOLUTION NMR STRUCTURE OF THE DIMERIZATION DOMAIN OF THE YEAST TRANSCRIPTIONAL ACTIVATOR GAL4 (RESIDUES 50-106)'''<br />
'''SOLUTION NMR STRUCTURE OF THE DIMERIZATION DOMAIN OF THE YEAST TRANSCRIPTIONAL ACTIVATOR GAL4 (RESIDUES 50-106)'''<br />


==Overview==
==Overview==
The GAL4 dimerization domain (GAL4-dd) is a powerful transcriptional, activator when tethered to DNA in a cell bearing a mutant of the GAL11, protein, named GAL11P. GAL11P (like GAL11) is a component of the, RNA-polymerase II holoenzyme. Nuclear magnetic resonance (NMR) studies of, GAL4-dd revealed an elongated dimer structure with C(2) symmetry, containing three helices that mediate dimerization via coiled-coil, contacts. The two loops between the three coiled coils form mobile bulges, causing a variation of twist angles between the helix pairs. Chemical, shift perturbation analysis mapped the GAL11P-binding site to the, C-terminal helix alpha3 and the loop between alpha1 and alpha2. One GAL11P, monomer binds to one GAL4-dd dimer rendering the dimer asymmetric and, implying an extreme negative cooperativity mechanism. Alanine-scanning, mutagenesis of GAL4-dd showed that the NMR-derived GAL11P-binding face is, crucial for the novel transcriptional activating function of the GAL4-dd, on GAL11P interaction. The binding of GAL4 to GAL11P, although an, artificial interaction, represents a unique structural motif for an, activating region capable of binding to a single target to effect gene, expression.
The GAL4 dimerization domain (GAL4-dd) is a powerful transcriptional activator when tethered to DNA in a cell bearing a mutant of the GAL11 protein, named GAL11P. GAL11P (like GAL11) is a component of the RNA-polymerase II holoenzyme. Nuclear magnetic resonance (NMR) studies of GAL4-dd revealed an elongated dimer structure with C(2) symmetry containing three helices that mediate dimerization via coiled-coil contacts. The two loops between the three coiled coils form mobile bulges causing a variation of twist angles between the helix pairs. Chemical shift perturbation analysis mapped the GAL11P-binding site to the C-terminal helix alpha3 and the loop between alpha1 and alpha2. One GAL11P monomer binds to one GAL4-dd dimer rendering the dimer asymmetric and implying an extreme negative cooperativity mechanism. Alanine-scanning mutagenesis of GAL4-dd showed that the NMR-derived GAL11P-binding face is crucial for the novel transcriptional activating function of the GAL4-dd on GAL11P interaction. The binding of GAL4 to GAL11P, although an artificial interaction, represents a unique structural motif for an activating region capable of binding to a single target to effect gene expression.


==About this Structure==
==About this Structure==
1HBW 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HBW OCA].  
1HBW 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=1HBW OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ansari, A.Z.]]
[[Category: Ansari, A Z.]]
[[Category: Farrell, S.]]
[[Category: Farrell, S.]]
[[Category: Hare, B.]]
[[Category: Hare, B.]]
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[[Category: Ptashne, M.]]
[[Category: Ptashne, M.]]
[[Category: Schmidt, P.]]
[[Category: Schmidt, P.]]
[[Category: Shin, E.J.]]
[[Category: Shin, E J.]]
[[Category: Simkovic, N.]]
[[Category: Simkovic, N.]]
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
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[[Category: transcriptional activator]]
[[Category: transcriptional activator]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:38 2008''