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1hbw

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Revision as of 11:06, 31 March 2021

Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106)

Structural highlights

1hbw is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1aw6, 1d66
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hidalgo P, Ansari AZ, Schmidt P, Hare B, Simkovich N, Farrell S, Shin EJ, Ptashne M, Wagner G. Recruitment of the transcriptional machinery through GAL11P: structure and interactions of the GAL4 dimerization domain. Genes Dev. 2001 Apr 15;15(8):1007-20. PMID:11316794 doi:10.1101/gad.873901

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hbw"

@@ Line 3: / Line 3: @@
 <StructureSection load='1hbw' size='340' side='right'caption='[[1hbw]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hbw]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HBW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hbw]] is a 2 chain structure. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aw6|1aw6]], [[1d66|1d66]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aw6|1aw6]], [[1d66|1d66]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hbw OCA], [http://pdbe.org/1hbw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hbw RCSB], [http://www.ebi.ac.uk/pdbsum/1hbw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hbw ProSAT]</span></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 ==
-[[http://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.
+[[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 ==
@@ Line 21: / Line 21: @@
 ==See Also==
 *[[Gal3-Gal80-Gal4|Gal3-Gal80-Gal4]]
-*[[User:Wayne Decatur/Gal 4|User:Wayne Decatur/Gal 4]]
 == References ==
 <references/>

1hbw

From Proteopedia

Revision as of 11:06, 31 March 2021

Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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