4eag - Revision history

OCA at 13:46, 8 November 2023

2023-11-08T13:46:45Z

← Older revision		Revision as of 13:46, 8 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eag]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eag]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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]] 2.701Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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=4eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eag OCA], [https://pdbe.org/4eag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eag RCSB], [https://www.ebi.ac.uk/pdbsum/4eag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eag 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=4eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eag OCA], [https://pdbe.org/4eag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eag RCSB], [https://www.ebi.ac.uk/pdbsum/4eag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eag ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/O18645_DROME O18645_DROME]]		[https://www.uniprot.org/uniprot/O18645_DROME O18645_DROME]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:00, 28 September 2022

2022-09-28T07:00:10Z

← Older revision		Revision as of 07:00, 28 September 2022
Line 1:		Line 1:

	==Co-crystal structure of an chimeric AMPK core with ATP==		==Co-crystal structure of an chimeric AMPK core with ATP==
	<StructureSection load='4eag' size='340' side='right' caption='[[4eag]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='4eag' size='340' side='right'caption='[[4eag]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eag]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~] and [~~http~~://en.wikipedia.org/wiki/~~Drome Drome~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EAG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eag]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eai\|4eai]], [[4eaj\|4eaj]], [[4eak\|4eak]], [[4eal\|4eal]]</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=4eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eag OCA], [https://pdbe.org/4eag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eag RCSB], [https://www.ebi.ac.uk/pdbsum/4eag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eag ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1A, EG:132E8.2, SNF1A-RA, CG3051, Dmel_CG3051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Prkab1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Prkag1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eag OCA], [~~http~~://pdbe.org/4eag PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4eag RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4eag PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4eag ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/~~AAKG1_RAT AAKG1_RAT~~]] AMP/ATP-binding subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. 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 (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:17851531</ref> <ref>PMID:21399626</ref> [[http://www.uniprot.org/uniprot/AAKB1_RAT AAKB1_RAT]] Non-catalytic subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).		[[https://www.uniprot.org/uniprot/O18645_DROME O18645_DROME]]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4eag" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4eag" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[AMP-activated protein kinase 3D structures\|AMP-activated protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Buffalo rat~~]]		[[Category: Drosophila melanogaster]]
	[[Category: ~~Drome~~]]		[[Category: Large Structures]]
	[[Category: Chen, L]]		[[Category: Rattus norvegicus]]
	[[Category: Neumann, D]]		[[Category: Chen L]]
	[[Category: Schlattner, U]]		[[Category: Neumann D]]
	[[Category: Wang, J]]		[[Category: Schlattner U]]
	[[Category: Wang, Z X]]		[[Category: Wang J]]
	[[Category: Wu, J W]]		[[Category: Wang Z-X]]
	[[Category: Yan~~, S F~~]]		[[Category: Wu J-W]]
	[[Category: Zhang, Y Y]]		[[Category: Yan SF]]
	~~[[Category: Ampk]]~~		[[Category: Zhang Y-Y]]
	~~[[Category: Transferase~~]]

OCA at 19:54, 4 August 2016

2016-08-04T19:54:41Z

← Older revision		Revision as of 19:54, 4 August 2016
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	==Co-crystal structure of an chimeric AMPK core with ATP==		==Co-crystal structure of an chimeric AMPK core with ATP==
	<StructureSection load='4eag' size='340' side='right' caption='[[4eag]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='4eag' size='340' side='right' caption='[[4eag]], [[Resolution\|resolution]] 2.70Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eai\|4eai]], [[4eaj\|4eaj]], [[4eak\|4eak]], [[4eal\|4eal]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eai\|4eai]], [[4eaj\|4eaj]], [[4eak\|4eak]], [[4eal\|4eal]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1A, EG:132E8.2, SNF1A-RA, CG3051, Dmel_CG3051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Prkab1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Prkag1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1A, EG:132E8.2, SNF1A-RA, CG3051, Dmel_CG3051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Prkab1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Prkag1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eag RCSB], [http://www.ebi.ac.uk/pdbsum/4eag 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=4eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eag OCA], [http://pdbe.org/4eag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eag RCSB], [http://www.ebi.ac.uk/pdbsum/4eag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eag ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4eag" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:36, 25 December 2014

2014-12-25T12:36:40Z

← Older revision		Revision as of 12:36, 25 December 2014
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	~~{{STRUCTURE_4eag\| PDB=4eag \| SCENE= }}~~		==Co-crystal structure of an chimeric AMPK core with ATP==
	===Co-crystal structure of an chimeric AMPK core with ATP===		<StructureSection load='4eag' size='340' side='right' caption='[[4eag]], [[Resolution\|resolution]] 2.70Å' scene=''>
	~~{{ABSTRACT_PUBMED_22659875}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4eag]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EAG FirstGlance]. <br>
	==Function==		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eai\|4eai]], [[4eaj\|4eaj]], [[4eak\|4eak]], [[4eal\|4eal]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNF1A, EG:132E8.2, SNF1A-RA, CG3051, Dmel_CG3051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Prkab1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Prkag1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4eag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eag RCSB], [http://www.ebi.ac.uk/pdbsum/4eag PDBsum]</span></td></tr>
			</table>
			== Function ==
	[[http://www.uniprot.org/uniprot/AAKG1_RAT AAKG1_RAT]] AMP/ATP-binding subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. 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 (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:17851531</ref> <ref>PMID:21399626</ref> [[http://www.uniprot.org/uniprot/AAKB1_RAT AAKB1_RAT]] Non-catalytic subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).		[[http://www.uniprot.org/uniprot/AAKG1_RAT AAKG1_RAT]] AMP/ATP-binding subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. 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 (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:17851531</ref> <ref>PMID:21399626</ref> [[http://www.uniprot.org/uniprot/AAKB1_RAT AAKB1_RAT]] Non-catalytic subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the gamma subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the gamma subunit in the presence of ATP. However, site 3 is occupied in the presence of AMP. Mutagenesis studies indicate that sites 3 and 4 are important for AMPK allosteric activation.

	~~==About this Structure==~~		AMP-activated protein kinase undergoes nucleotide-dependent conformational changes.,Chen L, Wang J, Zhang YY, Yan SF, Neumann D, Schlattner U, Wang ZX, Wu JW Nat Struct Mol Biol. 2012 Jun 3;19(7):716-8. doi: 10.1038/nsmb.2319. PMID:22659875<ref>PMID:22659875</ref>
	~~[[4eag]] is a~~ 3 ~~chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Buffalo_rat Buffalo rat] and [http:/~~/en.~~wikipedia~~.~~org/wiki/Drome Drome]. Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA].~~

	==~~Reference~~==		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~<ref group="xtra">PMID:022659875</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
	[[Category: Drome]]		[[Category: Drome]]
	[[Category: Chen, L.]]		[[Category: Chen, L]]
	[[Category: Neumann, D.]]		[[Category: Neumann, D]]
	[[Category: Schlattner, U.]]		[[Category: Schlattner, U]]
	[[Category: Wang, J.]]		[[Category: Wang, J]]
	[[Category: Wang, Z X.]]		[[Category: Wang, Z X]]
	[[Category: Wu, J W.]]		[[Category: Wu, J W]]
	[[Category: Yan, S F.]]		[[Category: Yan, S F]]
	[[Category: Zhang, Y Y.]]		[[Category: Zhang, Y Y]]
	[[Category: Ampk]]		[[Category: Ampk]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 13:41, 12 March 2014

2014-03-12T13:41:18Z

← Older revision		Revision as of 13:41, 12 March 2014
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	~~[[Image:4eag.jpg\|left\|200px]]~~

	~~<!--~~
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	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
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	{{STRUCTURE_4eag\| PDB=4eag \| SCENE= }}		{{STRUCTURE_4eag\| PDB=4eag \| SCENE= }}

	===Co-crystal structure of an chimeric AMPK core with ATP===		===Co-crystal structure of an chimeric AMPK core with ATP===
			{{ABSTRACT_PUBMED_22659875}}

			==Function==
			[[http://www.uniprot.org/uniprot/AAKG1_RAT AAKG1_RAT]] AMP/ATP-binding subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. 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 (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.<ref>PMID:17851531</ref> <ref>PMID:21399626</ref> [[http://www.uniprot.org/uniprot/AAKB1_RAT AAKB1_RAT]] Non-catalytic subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

	==About this Structure==		==About this Structure==
	[[4eag]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Drosophila_melanogaster Drosophila melanogaster~~] and [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA].		[[4eag]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAG OCA].
	[[Category: ~~Drosophila melanogaster~~]]
	[[Category: ~~Rattus norvegicus~~]]		==Reference==
			<ref group="xtra">PMID:022659875</ref><references group="xtra"/><references/>
			[[Category: Buffalo rat]]
			[[Category: Drome]]
	[[Category: Chen, L.]]		[[Category: Chen, L.]]
	[[Category: Neumann, D.]]		[[Category: Neumann, D.]]

OCA at 07:55, 6 June 2012

2012-06-06T07:55:26Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:4eag.jpg|left|200px]]
-The entry 4eag is ON HOLD  until Paper Publication
+<!--
-Authors: Chen, L., Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X., Wu, J.-W.
+===Co-crystal structure of an chimeric AMPK core with ATP===
-Description: Co-crystal structure of an chimeric AMPK core with ATP

OCA at 06:40, 11 April 2012

2012-04-11T06:40:04Z

← Older revision		Revision as of 06:40, 11 April 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4eag is ON HOLD		The entry 4eag is ON HOLD until Paper Publication

	Authors: Chen, L., Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X., Wu, J.-W.		Authors: Chen, L., Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X., Wu, J.-W.

	Description: Co-crystal structure of an chimeric AMPK core with ATP		Description: Co-crystal structure of an chimeric AMPK core with ATP

OCA at 05:46, 4 April 2012

2012-04-04T05:46:43Z

← Older revision		Revision as of 05:46, 4 April 2012
Line 3:		Line 3:
	The entry 4eag is ON HOLD		The entry 4eag is ON HOLD

	Authors: Chen,L. , Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X, Wu, J.-W.		Authors: Chen, L., Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X., Wu, J.-W.

	Description: Co-crystal structure of an chimeric AMPK core with ATP		Description: Co-crystal structure of an chimeric AMPK core with ATP

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

2012-03-28T07:26:42Z

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

← Older revision	Revision as of 07:26, 28 March 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4eag is ON HOLD Authors: Chen,L. , Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X, Wu, J.-W. Description: Co-crystal st...

2012-03-28T07:26:41Z

New page: '''Unreleased structure''' The entry 4eag is ON HOLD Authors: Chen,L. , Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X, Wu, J.-W. Description: Co-crystal st...

New page

'''Unreleased structure'''

The entry 4eag is ON HOLD

Authors: Chen,L. , Wang, J., Zhang, Y.-Y., Yan, S.F., Neumann, D., Schlattner, U., Wang, Z.-X, Wu, J.-W.

Description: Co-crystal structure of an chimeric AMPK core with ATP