View source for 1hbw


==Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106)==
<StructureSection load='1hbw' size='340' side='right'caption='[[1hbw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hbw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HBW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hbw OCA], [https://pdbe.org/1hbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hbw RCSB], [https://www.ebi.ac.uk/pdbsum/1hbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hbw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GAL4_YEAST GAL4_YEAST] This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which code for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of these genes.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Recruitment of the transcriptional machinery through GAL11P: structure and interactions of the GAL4 dimerization domain.,Hidalgo P, Ansari AZ, Schmidt P, Hare B, Simkovich N, Farrell S, Shin EJ, Ptashne M, Wagner G Genes Dev. 2001 Apr 15;15(8):1007-20. PMID:11316794<ref>PMID:11316794</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hbw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Gal3-Gal80-Gal4|Gal3-Gal80-Gal4]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Ansari AZ]]
[[Category: Farrell S]]
[[Category: Hare B]]
[[Category: Hidalgo P]]
[[Category: Ptashne M]]
[[Category: Schmidt P]]
[[Category: Shin EJ]]
[[Category: Simkovic N]]
[[Category: Wagner G]]