4h62 - Revision history

OCA at 08:01, 3 November 2022

2022-11-03T08:01:50Z

←Older revision		Revision as of 08:01, 3 November 2022
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	==Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C==		==Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C==
-	<StructureSection load='4h62' size='340' side='right' caption='[[4h62]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='4h62' size='340' side='right'caption='[[4h62]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4h62]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Baker's_yeast Baker's yeast~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H62 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4H62 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4h62]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H62 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>~~</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=4h62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h62 OCA], [https://pdbe.org/4h62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h62 RCSB], [https://www.ebi.ac.uk/pdbsum/4h62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h62 ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4h61\|4h61]], [[4h63\|4h63]]</td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MED11, YM9718.11C, YMR112C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MED22, SRB6, YBR1721, YBR253W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MED17, SRB4, YER022W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4h62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h62 OCA], [~~http~~://pdbe.org/4h62 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4h62 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4h62 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4h62 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MED11_YEAST MED11_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex (PIC) with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The essential MED11/22 heterodimer specifically functions in promoting stable PIC formation.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:18691966</ref> [[http://www.uniprot.org/uniprot/MED17_YEAST MED17_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:11555651</ref> <ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:9845373</ref> [[http://www.uniprot.org/uniprot/MED22_YEAST MED22_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref>	+	[https://www.uniprot.org/uniprot/MED11_YEAST MED11_YEAST] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex (PIC) with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The essential MED11/22 heterodimer specifically functions in promoting stable PIC formation.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:18691966</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Baker's yeast~~]]	+	[[Category: Large Structures]]
-	[[Category: Cramer, P]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: Kurth, F]]	+	[[Category: Cramer P]]
-	[[Category: Lariviere, L]]	+	[[Category: Kurth F]]
-	[[Category: Plaschka, C]]	+	[[Category: Lariviere L]]
-	[[Category: Seizl, M]]	+	[[Category: Plaschka C]]
-	[[Category: Wenzeck, L]]	+	[[Category: Seizl M]]
-	~~[[Category: Mediator complex]]~~	+	[[Category: Wenzeck L]]
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 08:24, 4 August 2016

2016-08-04T08:24:08Z

←Older revision		Revision as of 08:24, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C==		==Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C==
	<StructureSection load='4h62' size='340' side='right' caption='[[4h62]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='4h62' size='340' side='right' caption='[[4h62]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4h62]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H62 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H62 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4h62]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H62 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H62 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4h61\|4h61]], [[4h63\|4h63]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4h61\|4h61]], [[4h63\|4h63]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MED11, YM9718.11C, YMR112C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~]), MED22, SRB6, YBR1721, YBR253W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~]), MED17, SRB4, YER022W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MED11, YM9718.11C, YMR112C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MED22, SRB6, YBR1721, YBR253W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MED17, SRB4, YER022W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4h62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h62 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h62 RCSB], [http://www.ebi.ac.uk/pdbsum/4h62 PDBsum]</span></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=4h62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h62 OCA], [http://pdbe.org/4h62 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h62 RCSB], [http://www.ebi.ac.uk/pdbsum/4h62 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h62 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/MED17_YEAST MED17_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:11555651</ref> <ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:9845373</ref>	+	[[http://www.uniprot.org/uniprot/MED11_YEAST MED11_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex (PIC) with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The essential MED11/22 heterodimer specifically functions in promoting stable PIC formation.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:18691966</ref> [[http://www.uniprot.org/uniprot/MED17_YEAST MED17_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:11555651</ref> <ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:9845373</ref> [[http://www.uniprot.org/uniprot/MED22_YEAST MED22_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4h62" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Saccharomyces cerevisiae s288c~~]]	+	[[Category: Baker's yeast]]
	[[Category: Cramer, P]]		[[Category: Cramer, P]]
	[[Category: Kurth, F]]		[[Category: Kurth, F]]

OCA at 07:19, 25 December 2014

2014-12-25T07:19:01Z

←Older revision		Revision as of 07:19, 25 December 2014
Line 9:		Line 9:
	<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=4h62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h62 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h62 RCSB], [http://www.ebi.ac.uk/pdbsum/4h62 PDBsum]</span></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=4h62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h62 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h62 RCSB], [http://www.ebi.ac.uk/pdbsum/4h62 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MED17_YEAST MED17_YEAST]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.<ref>PMID:11555651</ref> <ref>PMID:16076843</ref> <ref>PMID:16263706</ref> <ref>PMID:16885025</ref> <ref>PMID:9845373</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 09:54, 10 December 2014

2014-12-10T09:54:46Z

←Older revision		Revision as of 09:54, 10 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4h62.~~png~~\|~~left~~\|~~200px~~]]	+	==Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C==
		+	<StructureSection load='4h62' size='340' side='right' caption='[[4h62]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4h62]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H62 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H62 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4h61\|4h61]], [[4h63\|4h63]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MED11, YM9718.11C, YMR112C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), MED22, SRB6, YBR1721, YBR253W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), MED17, SRB4, YER022W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=4h62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h62 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h62 RCSB], [http://www.ebi.ac.uk/pdbsum/4h62 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Gene transcription by RNA polymerase (Pol) II requires the coactivator complex Mediator. Mediator connects transcriptional regulators and Pol II, and is linked to human disease. Mediator from the yeast Saccharomyces cerevisiae has a molecular mass of 1.4 megadaltons and comprises 25 subunits that form the head, middle, tail and kinase modules. The head module constitutes one-half of the essential Mediator core, and comprises the conserved subunits Med6, Med8, Med11, Med17, Med18, Med20 and Med22. Recent X-ray analysis of the S. cerevisiae head module at 4.3 A resolution led to a partial architectural model with three submodules called neck, fixed jaw and moveable jaw. Here we determine de novo the crystal structure of the head module from the fission yeast Schizosaccharomyces pombe at 3.4 A resolution. Structure solution was enabled by new structures of Med6 and the fixed jaw, and previous structures of the moveable jaw and part of the neck, and required deletion of Med20. The S. pombe head module resembles the head of a crocodile with eight distinct elements, of which at least four are mobile. The fixed jaw comprises tooth and nose domains, whereas the neck submodule contains a helical spine and one limb, with shoulder, arm and finger elements. The arm and the essential shoulder contact other parts of Mediator. The jaws and a central joint are implicated in interactions with Pol II and its carboxy-terminal domain, and the joint is required for transcription in vitro. The S. pombe head module structure leads to a revised model of the S. cerevisiae module, reveals a high conservation and flexibility, explains known mutations, and provides the basis for unravelling a central mechanism of gene regulation.

-	~~{{STRUCTURE_4h62\| PDB=4h62 \| SCENE= }}~~	+	Structure of the Mediator head module.,Lariviere L, Plaschka C, Seizl M, Wenzeck L, Kurth F, Cramer P Nature. 2012 Oct 31. doi: 10.1038/nature11670. PMID:23123849<ref>PMID:23123849</ref>

-	~~===Structure~~ of the ~~Saccharomyces cerevisiae Mediator subcomplex Med17C~~/~~Med11C/Med22C===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_23123849}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[4h62]] is a 3 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H62 OCA].~~	+	</StructureSection>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
-	[[Category: Cramer, P.]]	+	[[Category: Cramer, P]]
-	[[Category: Kurth, F.]]	+	[[Category: Kurth, F]]
-	[[Category: Lariviere, L.]]	+	[[Category: Lariviere, L]]
-	[[Category: Plaschka, C.]]	+	[[Category: Plaschka, C]]
-	[[Category: Seizl, M.]]	+	[[Category: Seizl, M]]
-	[[Category: Wenzeck, L.]]	+	[[Category: Wenzeck, L]]
	[[Category: Mediator complex]]		[[Category: Mediator complex]]
	[[Category: Nucleus]]		[[Category: Nucleus]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 10:07, 5 December 2012

2012-12-05T10:07:50Z

←Older revision		Revision as of 10:07, 5 December 2012
Line 1:		Line 1:
-	[[Image:4h62.~~jpg~~\|left\|200px]]	+	[[Image:4h62.png\|left\|200px]]

	{{STRUCTURE_4h62\| PDB=4h62 \| SCENE= }}		{{STRUCTURE_4h62\| PDB=4h62 \| SCENE= }}
Line 5:		Line 5:
	===Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C===		===Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C===

		+	{{ABSTRACT_PUBMED_23123849}}

	==About this Structure==		==About this Structure==

OCA at 09:27, 31 October 2012

2012-10-31T09:27:03Z

←Older revision		Revision as of 09:27, 31 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4h62.jpg\|left\|200px]]

-	~~The entry~~ 4h62 ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4h62\| PDB=4h62 \| SCENE= }}

-	~~Authors: Lariviere, L., Plaschka, C., Seizl, M., Wenzeck, L., Kurth, F., Cramer, P.~~	+	===Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C===

-	~~Description:~~ Structure ~~of the~~ Saccharomyces cerevisiae ~~Mediator subcomplex Med17C~~/~~Med11C~~/~~Med22C~~	+
		+	==About this Structure==
		+	[[4h62]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H62 OCA].
		+	[[Category: Saccharomyces cerevisiae s288c]]
		+	[[Category: Cramer, P.]]
		+	[[Category: Kurth, F.]]
		+	[[Category: Lariviere, L.]]
		+	[[Category: Plaschka, C.]]
		+	[[Category: Seizl, M.]]
		+	[[Category: Wenzeck, L.]]
		+	[[Category: Mediator complex]]
		+	[[Category: Nucleus]]
		+	[[Category: Transcription]]

OCA at 05:48, 3 October 2012

2012-10-03T05:48:12Z

←Older revision		Revision as of 05:48, 3 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4h62 is ON HOLD	+	The entry 4h62 is ON HOLD until Paper Publication

	Authors: Lariviere, L., Plaschka, C., Seizl, M., Wenzeck, L., Kurth, F., Cramer, P.		Authors: Lariviere, L., Plaschka, C., Seizl, M., Wenzeck, L., Kurth, F., Cramer, P.

	Description: Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C		Description: Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C

OCA: Protected "4h62" [edit=sysop:move=sysop]

2012-09-26T20:13:46Z

Protected "4h62" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:13, 26 September 2012

OCA: New page: '''Unreleased structure''' The entry 4h62 is ON HOLD Authors: Lariviere, L., Plaschka, C., Seizl, M., Wenzeck, L., Kurth, F., Cramer, P. Description: Structure of the Saccharomyces cer...

2012-09-26T20:13:45Z

New page: '''Unreleased structure''' The entry 4h62 is ON HOLD Authors: Lariviere, L., Plaschka, C., Seizl, M., Wenzeck, L., Kurth, F., Cramer, P. Description: Structure of the Saccharomyces cer...

New page

'''Unreleased structure'''

The entry 4h62 is ON HOLD

Authors: Lariviere, L., Plaschka, C., Seizl, M., Wenzeck, L., Kurth, F., Cramer, P.

Description: Structure of the Saccharomyces cerevisiae Mediator subcomplex Med17C/Med11C/Med22C