Farmer 2 gal4sandbox - Revision history

Ann Taylor at 23:26, 1 September 2015

Ann Taylor — Tue, 01 Sep 2015 23:26:53 GMT

←Older revision		Revision as of 23:26, 1 September 2015
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	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into 3 distinct modules: A compact, <scene name='71/711060/Metal_binding_domain/1'>~~metal binding domain~~</scene>, and an <scene name='71/711060/Extended_linker/1'>extended linker</scene> (41-49), and an <scene name='71/711060/Dimerization_element/1'>alpha-helical dimerization element</scene> (50-64). A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.	+	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into 3 distinct modules: A compact, <scene name='71/711060/Metal_binding_domain/2'>Metal Binding Domain</scene>, and an <scene name='71/711060/Extended_linker/1'>extended linker</scene> (41-49), and an <scene name='71/711060/Dimerization_element/1'>alpha-helical dimerization element</scene> (50-64). A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

	DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>		DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>

Ann Taylor at 23:21, 1 September 2015

Ann Taylor — Tue, 01 Sep 2015 23:21:27 GMT

←Older revision		Revision as of 23:21, 1 September 2015
Line 20:		Line 20:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into 3 distinct modules: A compact, <scene name='71/711060/Metal_binding_domain/1'>metal binding domain</scene>, and an <scene name='71/711060/Extended_linker/1'>extended linker</scene> (41-49), and an alpha-helical dimerization element (50-64). A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.	+	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into 3 distinct modules: A compact, <scene name='71/711060/Metal_binding_domain/1'>metal binding domain</scene>, and an <scene name='71/711060/Extended_linker/1'>extended linker</scene> (41-49), and an <scene name='71/711060/Dimerization_element/1'>alpha-helical dimerization element</scene> (50-64). A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

	DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>		DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>

Ann Taylor at 23:17, 1 September 2015

Ann Taylor — Tue, 01 Sep 2015 23:17:29 GMT

←Older revision		Revision as of 23:17, 1 September 2015
Line 20:		Line 20:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into 3 distinct modules: A compact, <scene name='71/711060/Metal_binding_domain/1'>metal binding domain</scene>, and an extended linker, and an alpha-helical dimerization element. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.	+	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into 3 distinct modules: A compact, <scene name='71/711060/Metal_binding_domain/1'>metal binding domain</scene>, and an <scene name='71/711060/Extended_linker/1'>extended linker</scene> (41-49), and an alpha-helical dimerization element (50-64). A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

	DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>		DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>

Ann Taylor at 23:07, 1 September 2015

Ann Taylor — Tue, 01 Sep 2015 23:07:43 GMT

←Older revision		Revision as of 23:07, 1 September 2015
Line 20:		Line 20:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. <scene name='71/711060/Metal_binding_domain/1'>metal binding domain</scene>A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.	+	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. Each subunit folds into 3 distinct modules: A compact, <scene name='71/711060/Metal_binding_domain/1'>metal binding domain</scene>, and an extended linker, and an alpha-helical dimerization element. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

	DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>		DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>

Ann Taylor at 23:05, 1 September 2015

Ann Taylor — Tue, 01 Sep 2015 23:05:09 GMT

←Older revision		Revision as of 23:05, 1 September 2015
Line 20:		Line 20:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.	+	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. <scene name='71/711060/Metal_binding_domain/1'>metal binding domain</scene>A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

	DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>		DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>

Ann Taylor at 22:52, 1 September 2015

Ann Taylor — Tue, 01 Sep 2015 22:52:14 GMT

←Older revision		Revision as of 22:52, 1 September 2015
Line 20:		Line 20:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.	+	A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a <scene name='71/711060/Dimer/1'>dimer</scene> to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

	DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>		DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>

Ann Taylor: New page: ==DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX== ==...

Ann Taylor — Tue, 01 Sep 2015 13:19:42 GMT

New page: ==DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX== <StructureSection load='1d66' size='340' side='right' caption='1d66, resolution 2.70Å' scene=''> ==...

New page

==DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX==
<StructureSection load='1d66' size='340' side='right' caption='[[1d66]], [[Resolution|resolution]] 2.70Å' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d66]] is a 4 chain structure with 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=1D66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D66 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=1d66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d66 RCSB], [http://www.ebi.ac.uk/pdbsum/1d66 PDBsum]</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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
<jmolCheckbox>
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d6/1d66_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

DNA recognition by GAL4: structure of a protein-DNA complex.,Marmorstein R, Carey M, Ptashne M, Harrison SC Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122<ref>PMID:1557122</ref>

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

==See Also==
*[[FirstGlance in Jmol|FirstGlance in Jmol]]
*[[Gal3-Gal80-Gal4|Gal3-Gal80-Gal4]]
*[[Hydrogen in macromolecular models|Hydrogen in macromolecular models]]
*[[User:Eric Martz/Introduction to Structural Bioinformatics I|User:Eric Martz/Introduction to Structural Bioinformatics I]]
*[[User:Eric Martz/Introduction to Structural Bioinformatics I%2C 2014|User:Eric Martz/Introduction to Structural Bioinformatics I%2C 2014]]
*[[User:Eric Martz/JSmol Notes|User:Eric Martz/JSmol Notes]]
*[[User:Wayne Decatur/Biochem642 Molecular Visualization 2010 Fall Sessions|User:Wayne Decatur/Biochem642 Molecular Visualization 2010 Fall Sessions]]
*[[User:Wayne Decatur/Biochem642 Molecular Visualization Sessions|User:Wayne Decatur/Biochem642 Molecular Visualization Sessions]]
*[[User:Wayne Decatur/UNH BCHEM833 Structural Analysis Workshop Session Fall 2012|User:Wayne Decatur/UNH BCHEM833 Structural Analysis Workshop Session Fall 2012]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Saccharomyces cerevisiae]]
[[Category: Carey, M]]
[[Category: Harrison, S C]]
[[Category: Marmorstein, R]]
[[Category: Ptashne, M]]
[[Category: Double helix]]
[[Category: Protein-dna complex]]
[[Category: Transcription-dna complex]]