3te5 - Revision history

OCA at 10:08, 1 March 2024

OCA — Fri, 01 Mar 2024 10:08:15 GMT

←Older revision		Revision as of 10:08, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3te5' size='340' side='right'caption='[[3te5]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3te5' size='340' side='right'caption='[[3te5]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3te5]] is a 3 chain structure with sequence from [https://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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3te5]] 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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NAI:1~~,~~4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.5Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3tdh\|3tdh]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=559292 Baker's yeast]), SIP2, SPM2, YGL208W, G1155 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SNF4, CAT3, YGL115W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>	+
-	~~<tr id='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase]~~, ~~with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1]~~ </~~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=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [https://pdbe.org/3te5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [https://www.ebi.ac.uk/pdbsum/3te5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3te5 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=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [https://pdbe.org/3te5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [https://www.ebi.ac.uk/pdbsum/3te5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3te5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SNF1_YEAST SNF1_YEAST]] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.<ref>PMID:15719021</ref> [[https://www.uniprot.org/uniprot/AAKG_YEAST AAKG_YEAST]] Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.<ref>PMID:10099331</ref> <ref>PMID:10224244</ref> <ref>PMID:11486005</ref> <ref>PMID:12393914</ref> <ref>PMID:12960168</ref> <ref>PMID:1468623</ref> <ref>PMID:18474591</ref> <ref>PMID:2169717</ref> <ref>PMID:22019086</ref> <ref>PMID:2557546</ref> <ref>PMID:3049551</ref> <ref>PMID:3939253</ref> <ref>PMID:6392017</ref> <ref>PMID:7050076</ref> <ref>PMID:8224185</ref> <ref>PMID:8544831</ref> <ref>PMID:8985180</ref> <ref>PMID:9600950</ref> [[https://www.uniprot.org/uniprot/SIP2_YEAST SIP2_YEAST]] Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.<ref>PMID:10990457</ref> <ref>PMID:12562756</ref>	+	[https://www.uniprot.org/uniprot/SNF1_YEAST SNF1_YEAST] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.<ref>PMID:15719021</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The SNF1 protein kinase complex plays an essential role in regulating gene expression in response to the level of extracellular glucose in budding yeast. SNF1 shares structural and functional similarities with mammalian AMP-activated protein kinase. Both kinases are activated by phosphorylation on a threonine residue within the activation loop segment of the catalytic subunit. Here we show that ADP is the long-sought metabolite that activates SNF1 in response to glucose limitation by protecting the enzyme against dephosphorylation by Glc7, its physiologically relevant protein phosphatase. We also show that the regulatory subunit of SNF1 has two ADP binding sites. The tighter site binds AMP, ADP, and ATP competitively with NADH, whereas the weaker site does not bind NADH, but is responsible for mediating the protective effect of ADP on dephosphorylation. Mutagenesis experiments suggest that the general mechanism by which ADP protects against dephosphorylation is strongly conserved between SNF1 and AMPK.	+
-		+
-	ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase.,Mayer FV, Heath R, Underwood E, Sanders MJ, Carmena D, McCartney RR, Leiper FC, Xiao B, Jing C, Walker PA, Haire LF, Ogrodowicz R, Martin SR, Schmidt MC, Gamblin SJ, Carling D Cell Metab. 2011 Nov 2;14(5):707-14. Epub 2011 Oct 20. PMID:22019086<ref>PMID:22019086</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3te5" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Baker's yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Non-specific serine/threonine protein kinase~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: Carling, D]]	+	[[Category: Carling D]]
-	[[Category: Carmena, D]]	+	[[Category: Carmena D]]
-	[[Category: Gamblin~~, S J~~]]	+	[[Category: Gamblin SJ]]
-	[[Category: Haire~~, L F~~]]	+	[[Category: Haire LF]]
-	[[Category: Heath, R]]	+	[[Category: Heath R]]
-	[[Category: Jing, C]]	+	[[Category: Jing C]]
-	[[Category: Leiper~~, F C~~]]	+	[[Category: Leiper FC]]
-	[[Category: Martin~~, S R~~]]	+	[[Category: Martin SR]]
-	[[Category: Mayer~~, F V~~]]	+	[[Category: Mayer FV]]
-	[[Category: McCartney, R]]	+	[[Category: McCartney R]]
-	[[Category: Ogrodowicz, R]]	+	[[Category: Ogrodowicz R]]
-	[[Category: Sanders~~, M J~~]]	+	[[Category: Sanders MJ]]
-	[[Category: Schmidt~~, M C~~]]	+	[[Category: Schmidt MC]]
-	[[Category: Underwood, E]]	+	[[Category: Underwood E]]
-	[[Category: Walker~~, P A~~]]	+	[[Category: Walker PA]]
-	[[Category: Xiao, B]]	+	[[Category: Xiao B]]
-	~~[[Category: Cbs domain]]~~	+
-	~~[[Category: Cytosol]]~~	+
-	~~[[Category: Nucleotide binding]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 16:54, 6 July 2022

OCA — Wed, 06 Jul 2022 16:54:05 GMT

←Older revision		Revision as of 16:54, 6 July 2022
Line 1:		Line 1:

	==structure of the regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH==		==structure of the regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH==
-	<StructureSection load='3te5' size='340' side='right' caption='[[3te5]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='3te5' size='340' side='right'caption='[[3te5]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3te5]] 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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3te5]] is a 3 chain structure with sequence from [https://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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tdh\|3tdh]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tdh\|3tdh]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SIP2, SPM2, YGL208W, G1155 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SNF4, CAT3, YGL115W ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SIP2, SPM2, YGL208W, G1155 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SNF4, CAT3, YGL115W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [~~http~~://pdbe.org/3te5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3te5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3te5 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=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [https://pdbe.org/3te5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [https://www.ebi.ac.uk/pdbsum/3te5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3te5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SNF1_YEAST SNF1_YEAST]] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.<ref>PMID:15719021</ref> [[~~http~~://www.uniprot.org/uniprot/AAKG_YEAST AAKG_YEAST]] Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.<ref>PMID:10099331</ref> <ref>PMID:10224244</ref> <ref>PMID:11486005</ref> <ref>PMID:12393914</ref> <ref>PMID:12960168</ref> <ref>PMID:1468623</ref> <ref>PMID:18474591</ref> <ref>PMID:2169717</ref> <ref>PMID:22019086</ref> <ref>PMID:2557546</ref> <ref>PMID:3049551</ref> <ref>PMID:3939253</ref> <ref>PMID:6392017</ref> <ref>PMID:7050076</ref> <ref>PMID:8224185</ref> <ref>PMID:8544831</ref> <ref>PMID:8985180</ref> <ref>PMID:9600950</ref> [[~~http~~://www.uniprot.org/uniprot/SIP2_YEAST SIP2_YEAST]] Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.<ref>PMID:10990457</ref> <ref>PMID:12562756</ref>	+	[[https://www.uniprot.org/uniprot/SNF1_YEAST SNF1_YEAST]] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.<ref>PMID:15719021</ref> [[https://www.uniprot.org/uniprot/AAKG_YEAST AAKG_YEAST]] Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.<ref>PMID:10099331</ref> <ref>PMID:10224244</ref> <ref>PMID:11486005</ref> <ref>PMID:12393914</ref> <ref>PMID:12960168</ref> <ref>PMID:1468623</ref> <ref>PMID:18474591</ref> <ref>PMID:2169717</ref> <ref>PMID:22019086</ref> <ref>PMID:2557546</ref> <ref>PMID:3049551</ref> <ref>PMID:3939253</ref> <ref>PMID:6392017</ref> <ref>PMID:7050076</ref> <ref>PMID:8224185</ref> <ref>PMID:8544831</ref> <ref>PMID:8985180</ref> <ref>PMID:9600950</ref> [[https://www.uniprot.org/uniprot/SIP2_YEAST SIP2_YEAST]] Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.<ref>PMID:10990457</ref> <ref>PMID:12562756</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Baker's yeast]]		[[Category: Baker's yeast]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Carling, D]]		[[Category: Carling, D]]

OCA at 07:18, 5 August 2016

OCA — Fri, 05 Aug 2016 07:18:36 GMT

←Older revision		Revision as of 07:18, 5 August 2016
Line 1:		Line 1:
		+
	==structure of the regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH==		==structure of the regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH==
	<StructureSection load='3te5' size='340' side='right' caption='[[3te5]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3te5' size='340' side='right' caption='[[3te5]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3te5]] is a 3 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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3te5]] 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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tdh\|3tdh]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tdh\|3tdh]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~4932 Saccharomyces cerevisiae~~]), SIP2, SPM2, YGL208W, G1155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~4932 Saccharomyces cerevisiae~~]), SNF4, CAT3, YGL115W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~4932 Saccharomyces cerevisiae~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SIP2, SPM2, YGL208W, G1155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SNF4, CAT3, YGL115W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [http://www.ebi.ac.uk/pdbsum/3te5 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=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [http://pdbe.org/3te5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [http://www.ebi.ac.uk/pdbsum/3te5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3te5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/SNF1_YEAST SNF1_YEAST]] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.<ref>PMID:15719021</ref> [[http://www.uniprot.org/uniprot/~~SNF4_YEAST SNF4_YEAST~~]] Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.<ref>PMID:~~7050076~~</ref> <ref>PMID:~~6392017~~</ref> <ref>PMID:~~3939253~~</ref> <ref>PMID:~~3049551~~</ref> <ref>PMID:~~2557546~~</ref> <ref>PMID:~~2169717~~</ref> <ref>PMID:~~1468623~~</ref> <ref>PMID:~~8224185~~</ref> <ref>PMID:~~8544831~~</ref> <ref>PMID:~~8985180~~</ref> <ref>PMID:~~10099331~~</ref> <ref>PMID:~~9600950~~</ref> <ref>PMID:~~10224244~~</ref> <ref>PMID:~~11486005~~</ref> <ref>PMID:~~12393914~~</ref> <ref>PMID:~~12960168~~</ref> <ref>PMID:~~18474591~~</ref> <ref>PMID:~~22019086~~</ref> [[http://www.uniprot.org/uniprot/SIP2_YEAST SIP2_YEAST]] Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.<ref>PMID:10990457</ref> <ref>PMID:12562756</ref>	+	[[http://www.uniprot.org/uniprot/SNF1_YEAST SNF1_YEAST]] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.<ref>PMID:15719021</ref> [[http://www.uniprot.org/uniprot/AAKG_YEAST AAKG_YEAST]] Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.<ref>PMID:10099331</ref> <ref>PMID:10224244</ref> <ref>PMID:11486005</ref> <ref>PMID:12393914</ref> <ref>PMID:12960168</ref> <ref>PMID:1468623</ref> <ref>PMID:18474591</ref> <ref>PMID:2169717</ref> <ref>PMID:22019086</ref> <ref>PMID:2557546</ref> <ref>PMID:3049551</ref> <ref>PMID:3939253</ref> <ref>PMID:6392017</ref> <ref>PMID:7050076</ref> <ref>PMID:8224185</ref> <ref>PMID:8544831</ref> <ref>PMID:8985180</ref> <ref>PMID:9600950</ref> [[http://www.uniprot.org/uniprot/SIP2_YEAST SIP2_YEAST]] Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.<ref>PMID:10990457</ref> <ref>PMID:12562756</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 3te5" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Baker's yeast]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Saccharomyces cerevisiae]]
	[[Category: Carling, D]]		[[Category: Carling, D]]
	[[Category: Carmena, D]]		[[Category: Carmena, D]]

OCA at 16:48, 25 December 2014

OCA — Thu, 25 Dec 2014 16:48:49 GMT

←Older revision		Revision as of 16:48, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3te5]] is a 3 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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3te5]] is a 3 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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tdh\|3tdh]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tdh\|3tdh]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), SIP2, SPM2, YGL208W, G1155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), SNF4, CAT3, YGL115W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), SIP2, SPM2, YGL208W, G1155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), SNF4, CAT3, YGL115W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [http://www.ebi.ac.uk/pdbsum/3te5 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=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [http://www.ebi.ac.uk/pdbsum/3te5 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SNF1_YEAST SNF1_YEAST]] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.<ref>PMID:15719021</ref> [[http://www.uniprot.org/uniprot/SNF4_YEAST SNF4_YEAST]] Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.<ref>PMID:7050076</ref> <ref>PMID:6392017</ref> <ref>PMID:3939253</ref> <ref>PMID:3049551</ref> <ref>PMID:2557546</ref> <ref>PMID:2169717</ref> <ref>PMID:1468623</ref> <ref>PMID:8224185</ref> <ref>PMID:8544831</ref> <ref>PMID:8985180</ref> <ref>PMID:10099331</ref> <ref>PMID:9600950</ref> <ref>PMID:10224244</ref> <ref>PMID:11486005</ref> <ref>PMID:12393914</ref> <ref>PMID:12960168</ref> <ref>PMID:18474591</ref> <ref>PMID:22019086</ref> [[http://www.uniprot.org/uniprot/SIP2_YEAST SIP2_YEAST]] Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.<ref>PMID:10990457</ref> <ref>PMID:12562756</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 15:		Line 17:
	ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase.,Mayer FV, Heath R, Underwood E, Sanders MJ, Carmena D, McCartney RR, Leiper FC, Xiao B, Jing C, Walker PA, Haire LF, Ogrodowicz R, Martin SR, Schmidt MC, Gamblin SJ, Carling D Cell Metab. 2011 Nov 2;14(5):707-14. Epub 2011 Oct 20. PMID:22019086<ref>PMID:22019086</ref>		ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase.,Mayer FV, Heath R, Underwood E, Sanders MJ, Carmena D, McCartney RR, Leiper FC, Xiao B, Jing C, Walker PA, Haire LF, Ogrodowicz R, Martin SR, Schmidt MC, Gamblin SJ, Carling D Cell Metab. 2011 Nov 2;14(5):707-14. Epub 2011 Oct 20. PMID:22019086<ref>PMID:22019086</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 23:		Line 25:
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
-	[[Category: Carling, D.]]	+	[[Category: Carling, D]]
-	[[Category: Carmena, D.]]	+	[[Category: Carmena, D]]
-	[[Category: Gamblin, S J.]]	+	[[Category: Gamblin, S J]]
-	[[Category: Haire, L F.]]	+	[[Category: Haire, L F]]
-	[[Category: Heath, R.]]	+	[[Category: Heath, R]]
-	[[Category: Jing, C.]]	+	[[Category: Jing, C]]
-	[[Category: Leiper, F C.]]	+	[[Category: Leiper, F C]]
-	[[Category: Martin, S R.]]	+	[[Category: Martin, S R]]
-	[[Category: Mayer, F V.]]	+	[[Category: Mayer, F V]]
-	[[Category: McCartney, R.]]	+	[[Category: McCartney, R]]
-	[[Category: Ogrodowicz, R.]]	+	[[Category: Ogrodowicz, R]]
-	[[Category: Sanders, M J.]]	+	[[Category: Sanders, M J]]
-	[[Category: Schmidt, M C.]]	+	[[Category: Schmidt, M C]]
-	[[Category: Underwood, E.]]	+	[[Category: Underwood, E]]
-	[[Category: Walker, P A.]]	+	[[Category: Walker, P A]]
-	[[Category: Xiao, B.]]	+	[[Category: Xiao, B]]
	[[Category: Cbs domain]]		[[Category: Cbs domain]]
	[[Category: Cytosol]]		[[Category: Cytosol]]
	[[Category: Nucleotide binding]]		[[Category: Nucleotide binding]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 06:17, 5 June 2014

OCA — Thu, 05 Jun 2014 06:17:35 GMT

←Older revision		Revision as of 06:17, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3te5.~~png~~\|~~left~~\|~~200px~~]]	+	==structure of the regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH==
		+	<StructureSection load='3te5' size='340' side='right' caption='[[3te5]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3te5]] is a 3 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=3TE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TE5 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tdh\|3tdh]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1, CAT1, CCR1, GLC2, PAS14, YDR477W, D8035.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), SIP2, SPM2, YGL208W, G1155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), SNF4, CAT3, YGL115W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3te5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3te5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3te5 RCSB], [http://www.ebi.ac.uk/pdbsum/3te5 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The SNF1 protein kinase complex plays an essential role in regulating gene expression in response to the level of extracellular glucose in budding yeast. SNF1 shares structural and functional similarities with mammalian AMP-activated protein kinase. Both kinases are activated by phosphorylation on a threonine residue within the activation loop segment of the catalytic subunit. Here we show that ADP is the long-sought metabolite that activates SNF1 in response to glucose limitation by protecting the enzyme against dephosphorylation by Glc7, its physiologically relevant protein phosphatase. We also show that the regulatory subunit of SNF1 has two ADP binding sites. The tighter site binds AMP, ADP, and ATP competitively with NADH, whereas the weaker site does not bind NADH, but is responsible for mediating the protective effect of ADP on dephosphorylation. Mutagenesis experiments suggest that the general mechanism by which ADP protects against dephosphorylation is strongly conserved between SNF1 and AMPK.

-	~~<!-~~-	+	ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase.,Mayer FV, Heath R, Underwood E, Sanders MJ, Carmena D, McCartney RR, Leiper FC, Xiao B, Jing C, Walker PA, Haire LF, Ogrodowicz R, Martin SR, Schmidt MC, Gamblin SJ, Carling D Cell Metab. 2011 Nov 2;14(5):707-14. Epub 2011 Oct 20. PMID:22019086<ref>PMID:22019086</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3te5"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	-->	+
-	~~{{STRUCTURE_3te5\| PDB=3te5 \| SCENE= }}~~	+

-	~~===structure~~ of the ~~regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22019086}}, adds the Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 22019086 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_22019086}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3te5]] is a 3 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=3TE5 OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022019086<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]

OCA at 18:10, 23 November 2011

OCA — Wed, 23 Nov 2011 18:10:01 GMT

←Older revision		Revision as of 18:10, 23 November 2011
Line 1:		Line 1:
-	[[Image:3te5.~~jpg~~\|left\|200px]]	+	[[Image:3te5.png\|left\|200px]]

	<!--		<!--

OCA at 11:35, 9 November 2011

OCA — Wed, 09 Nov 2011 11:35:23 GMT

←Older revision		Revision as of 11:35, 9 November 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3te5.jpg\|left\|200px]]

-	The ~~entry 3te5~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3te5", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3te5\| PDB=3te5 \| SCENE= }}

-	Authors: Mayer, F.V., Heath, R., Underwood, E., Sanders, M.J., Carmena, D., McCartney, R., Leiper, F.C., Xiao, B., Jing, C., Walker, P.A., Haire, L.F., Ogrodowicz, R., Martin, S.R., Schmidt, M.C., Gamblin, S.J., Carling, D.	+	===structure of the regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH===

-	~~Description~~: ~~structure of~~ the ~~regulatory fragment of sacchromyces cerevisiae ampk in complex~~ with ~~NADH~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22019086}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22019086 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22019086}}
		+
		+	==About this Structure==
		+	[[3te5]] is a 3 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=3TE5 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022019086</ref><references group="xtra"/>
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Saccharomyces cerevisiae]]
		+	[[Category: Carling, D.]]
		+	[[Category: Carmena, D.]]
		+	[[Category: Gamblin, S J.]]
		+	[[Category: Haire, L F.]]
		+	[[Category: Heath, R.]]
		+	[[Category: Jing, C.]]
		+	[[Category: Leiper, F C.]]
		+	[[Category: Martin, S R.]]
		+	[[Category: Mayer, F V.]]
		+	[[Category: McCartney, R.]]
		+	[[Category: Ogrodowicz, R.]]
		+	[[Category: Sanders, M J.]]
		+	[[Category: Schmidt, M C.]]
		+	[[Category: Underwood, E.]]
		+	[[Category: Walker, P A.]]
		+	[[Category: Xiao, B.]]
		+	[[Category: Cbs domain]]
		+	[[Category: Cytosol]]
		+	[[Category: Nucleotide binding]]
		+	[[Category: Transferase]]

OCA: Protected "3te5" [edit=sysop:move=sysop]

OCA — Wed, 24 Aug 2011 07:10:48 GMT

Protected "3te5" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:10, 24 August 2011

OCA: New page: '''Unreleased structure''' The entry 3te5 is ON HOLD Authors: Mayer, F.V., Heath, R., Underwood, E., Sanders, M.J., Carmena, D., McCartney, R., Leiper, F.C., Xiao, B., Jing, C., Walker,...

OCA — Wed, 24 Aug 2011 07:10:47 GMT

New page: '''Unreleased structure''' The entry 3te5 is ON HOLD Authors: Mayer, F.V., Heath, R., Underwood, E., Sanders, M.J., Carmena, D., McCartney, R., Leiper, F.C., Xiao, B., Jing, C., Walker,...

New page

'''Unreleased structure'''

The entry 3te5 is ON HOLD

Authors: Mayer, F.V., Heath, R., Underwood, E., Sanders, M.J., Carmena, D., McCartney, R., Leiper, F.C., Xiao, B., Jing, C., Walker, P.A., Haire, L.F., Ogrodowicz, R., Martin, S.R., Schmidt, M.C., Gamblin, S.J., Carling, D.

Description: structure of the regulatory fragment of sacchromyces cerevisiae ampk in complex with NADH