4y0g - Revision history

OCA at 13:02, 1 March 2024

2024-03-01T13:02:18Z

←Older revision		Revision as of 13:02, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.6Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [https://pdbe.org/4y0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [https://www.ebi.ac.uk/pdbsum/4y0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0g 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=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [https://pdbe.org/4y0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [https://www.ebi.ac.uk/pdbsum/4y0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/AAKB2_RAT AAKB2_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) (By similarity).		[https://www.uniprot.org/uniprot/AAKB2_RAT AAKB2_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) (By similarity).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	AMPK-activated protein kinase (AMPK) is a alphabetagamma heterotrimer that is important in regulating energy metabolism in all eukaryotes. The beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate binding affinity. beta2-CBM binds linear carbohydrates with four-fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30-fold tighter. To understand these affinity differences, especially for branched carbohydrates, we determined the NMR solution structure of beta2-CBM in complex with the single alpha1,6 branched carbohydrate glucosyl-beta-cyclodextrin (gBCD) which supported the dynamic nature of the binding site, but resonance broadening prevented defining where the alpha1,6 branch bound. We therefore solved the X-ray crystal structures of beta1- and beta2-CBM, in complex with gBCD, to 1.7 A and 2.0 A respectively. The additional threonine (Thr-101) of beta2-CBM expands the size of the surrounding loop, creating a pocket that accommodates the alpha1,6 branch. Hydrogen bonds are formed between the alpha1,6 branch and the backbone of Trp-99 and Lys-102 side chain of beta2-CBM. In contrast the alpha1,6 branch could not be observed in the beta1-CBM structure, suggesting that it does not form a specific interaction. The orientation of gBCD bound to beta1- and beta2-CBM is supported by thermodynamic and kinetic data obtained through isothermal titration calorimetry and NMR. These results suggest that AMPK containing the muscle specific beta2-isoform may therefore have greater affinity to partially degraded glycogen.
-
-	Determinants of oligosaccharide specificity of the carbohydrate binding modules of AMP-activated protein kinase.,Mobbs JI, Koay A, Di Paolo A, Bieri M, Petrie EJ, Gorman MA, Doughty L, Parker MW, Stapleton D, Griffin MD, Gooley PR Biochem J. 2015 Mar 16. PMID:25774984<ref>PMID:25774984</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4y0g" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[AMP-activated protein kinase 3D structures\|AMP-activated protein kinase 3D structures]]		*[[AMP-activated protein kinase 3D structures\|AMP-activated protein kinase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 18:01, 26 April 2023

2023-04-26T18:01:04Z

←Older revision		Revision as of 18:01, 26 April 2023
Line 3:		Line 3:
	<StructureSection load='4y0g' size='340' side='right'caption='[[4y0g]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4y0g' size='340' side='right'caption='[[4y0g]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Prkab2 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [https://pdbe.org/4y0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [https://www.ebi.ac.uk/pdbsum/4y0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0g ProSAT]</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=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [~~http~~://pdbe.org/4y0g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4y0g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0g ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AAKB2_RAT AAKB2_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) (By similarity).	+	[https://www.uniprot.org/uniprot/AAKB2_RAT AAKB2_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) (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Gooley, P R~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Gorman, M A~~]]	+	[[Category: Gooley PR]]
-	[[Category: ~~Griffin, M~~]]	+	[[Category: Gorman MA]]
-	[[Category: ~~Mobbs, J]]~~	+	[[Category: Griffin M]]
-	~~[[Category: Parker,~~ M W]]	+	[[Category: Mobbs J]]
-	[[Category: ~~Ampk~~]]	+	[[Category: Parker MW]]
-	[[Category: ~~Carbohydrate binding module]]~~	+
-	~~[[Category: Protein binding~~]]	+

OCA at 23:35, 5 June 2019

2019-06-05T23:35:57Z

←Older revision		Revision as of 23:35, 5 June 2019
Line 1:		Line 1:

	==beta2 carbohydrate binding module (CBM) of AMP-activated protein kinase (AMPK)==		==beta2 carbohydrate binding module (CBM) of AMP-activated protein kinase (AMPK)==
-	<StructureSection load='4y0g' size='340' side='right' caption='[[4y0g]], [[Resolution\|resolution]] 1.60Å' scene=''>	+	<StructureSection load='4y0g' size='340' side='right'caption='[[4y0g]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Prkab2 ([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=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [http://pdbe.org/4y0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [http://www.ebi.ac.uk/pdbsum/4y0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0g ProSAT]</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=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [http://pdbe.org/4y0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [http://www.ebi.ac.uk/pdbsum/4y0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0g ProSAT]</span></td></tr>
	</table>		</table>
Line 20:		Line 21:

	==See Also==		==See Also==
-	*[[AMP-activated protein kinase\|AMP-activated protein kinase]]	+	*[[AMP-activated protein kinase 3D structures\|AMP-activated protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Gooley, P R]]		[[Category: Gooley, P R]]
	[[Category: Gorman, M A]]		[[Category: Gorman, M A]]
Line 32:		Line 35:
	[[Category: Ampk]]		[[Category: Ampk]]
	[[Category: Carbohydrate binding module]]		[[Category: Carbohydrate binding module]]
		+	[[Category: Protein binding]]

OCA at 01:51, 10 March 2017

2017-03-10T01:51:59Z

←Older revision		Revision as of 01:51, 10 March 2017
Line 1:		Line 1:
		+
	==beta2 carbohydrate binding module (CBM) of AMP-activated protein kinase (AMPK)==		==beta2 carbohydrate binding module (CBM) of AMP-activated protein kinase (AMPK)==
	<StructureSection load='4y0g' size='340' side='right' caption='[[4y0g]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4y0g' size='340' side='right' caption='[[4y0g]], [[Resolution\|resolution]] 1.60Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [http://www.ebi.ac.uk/pdbsum/4y0g 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=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [http://pdbe.org/4y0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [http://www.ebi.ac.uk/pdbsum/4y0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4y0g" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[AMP-activated protein kinase\|AMP-activated protein kinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:08, 8 April 2015

2015-04-08T11:08:34Z

←Older revision		Revision as of 11:08, 8 April 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==beta2 carbohydrate binding module (CBM) of AMP-activated protein kinase (AMPK)==
		+	<StructureSection load='4y0g' size='340' side='right' caption='[[4y0g]], [[Resolution\|resolution]] 1.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4y0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0G FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y0g RCSB], [http://www.ebi.ac.uk/pdbsum/4y0g PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AAKB2_RAT AAKB2_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) (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	AMPK-activated protein kinase (AMPK) is a alphabetagamma heterotrimer that is important in regulating energy metabolism in all eukaryotes. The beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate binding affinity. beta2-CBM binds linear carbohydrates with four-fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30-fold tighter. To understand these affinity differences, especially for branched carbohydrates, we determined the NMR solution structure of beta2-CBM in complex with the single alpha1,6 branched carbohydrate glucosyl-beta-cyclodextrin (gBCD) which supported the dynamic nature of the binding site, but resonance broadening prevented defining where the alpha1,6 branch bound. We therefore solved the X-ray crystal structures of beta1- and beta2-CBM, in complex with gBCD, to 1.7 A and 2.0 A respectively. The additional threonine (Thr-101) of beta2-CBM expands the size of the surrounding loop, creating a pocket that accommodates the alpha1,6 branch. Hydrogen bonds are formed between the alpha1,6 branch and the backbone of Trp-99 and Lys-102 side chain of beta2-CBM. In contrast the alpha1,6 branch could not be observed in the beta1-CBM structure, suggesting that it does not form a specific interaction. The orientation of gBCD bound to beta1- and beta2-CBM is supported by thermodynamic and kinetic data obtained through isothermal titration calorimetry and NMR. These results suggest that AMPK containing the muscle specific beta2-isoform may therefore have greater affinity to partially degraded glycogen.

-	~~The entry 4y0g is ON HOLD until Paper Publication~~	+	Determinants of oligosaccharide specificity of the carbohydrate binding modules of AMP-activated protein kinase.,Mobbs JI, Koay A, Di Paolo A, Bieri M, Petrie EJ, Gorman MA, Doughty L, Parker MW, Stapleton D, Griffin MD, Gooley PR Biochem J. 2015 Mar 16. PMID:25774984<ref>PMID:25774984</ref>

-	~~Authors: Mobbs~~, J.~~, Gorman, M~~.~~A., Parker, M.W., Gooley, P.R., Griffin, M~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: beta2 carbohydrate binding module (CBM) of AMP-activated protein kinase (AMPK)~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
-	[[Category: ~~Parker~~, M.W]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Gooley, P R]]
		+	[[Category: Gorman, M A]]
	[[Category: Griffin, M]]		[[Category: Griffin, M]]
-	[[Category: Gorman, M.A]]
	[[Category: Mobbs, J]]		[[Category: Mobbs, J]]
-	[[Category: ~~Gooley~~, ~~P.R~~]]	+	[[Category: Parker, M W]]
		+	[[Category: Ampk]]
		+	[[Category: Carbohydrate binding module]]

OCA at 09:58, 4 March 2015

2015-03-04T09:58:26Z

←Older revision		Revision as of 09:58, 4 March 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4y0g is ON HOLD	+	The entry 4y0g is ON HOLD until Paper Publication

	Authors: Mobbs, J., Gorman, M.A., Parker, M.W., Gooley, P.R., Griffin, M.		Authors: Mobbs, J., Gorman, M.A., Parker, M.W., Gooley, P.R., Griffin, M.

OCA: Protected "4y0g" [edit=sysop:move=sysop]

2015-02-12T10:57:39Z

Protected "4y0g" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:57, 12 February 2015

OCA: New page: '''Unreleased structure''' The entry 4y0g is ON HOLD Authors: Mobbs, J., Gorman, M.A., Parker, M.W., Gooley, P.R., Griffin, M. Description: beta2 carbohydrate binding module (CBM) of A...

2015-02-12T10:57:37Z

New page: '''Unreleased structure''' The entry 4y0g is ON HOLD Authors: Mobbs, J., Gorman, M.A., Parker, M.W., Gooley, P.R., Griffin, M. Description: beta2 carbohydrate binding module (CBM) of A...

New page

'''Unreleased structure'''

The entry 4y0g is ON HOLD

Authors: Mobbs, J., Gorman, M.A., Parker, M.W., Gooley, P.R., Griffin, M.

Description: beta2 carbohydrate binding module (CBM) of AMP-activated protein kinase (AMPK)
[[Category: Unreleased Structures]]
[[Category: Parker, M.W]]
[[Category: Griffin, M]]
[[Category: Gorman, M.A]]
[[Category: Mobbs, J]]
[[Category: Gooley, P.R]]