4ywd - Revision history

OCA at 08:08, 27 September 2023

OCA — Wed, 27 Sep 2023 08:08:27 GMT

←Older revision		Revision as of 08:08, 27 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ywd]] is a 1 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=4YWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YWD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ywd]] is a 1 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=4YWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YWD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</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]] 2.1Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [https://pdbe.org/4ywd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [https://www.ebi.ac.uk/pdbsum/4ywd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywd 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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [https://pdbe.org/4ywd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [https://www.ebi.ac.uk/pdbsum/4ywd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywd ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:29, 10 May 2023

OCA — Wed, 10 May 2023 07:29:06 GMT

←Older revision		Revision as of 07:29, 10 May 2023
Line 3:		Line 3:
	<StructureSection load='4ywd' size='340' side='right'caption='[[4ywd]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4ywd' size='340' side='right'caption='[[4ywd]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ywd]] is a 1 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=4YWD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4YWD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ywd]] is a 1 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=4YWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YWD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wy8\|4wy8]], [[4wy9\|4wy9]], [[4wyb\|4wyb]]</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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [https://pdbe.org/4ywd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [https://www.ebi.ac.uk/pdbsum/4ywd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywd ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pck1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] </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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [~~http~~://pdbe.org/4ywd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ywd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywd ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PCKGC_RAT PCKGC_RAT]] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.	+	[https://www.uniprot.org/uniprot/PCKGC_RAT PCKGC_RAT] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Balan, M D~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Holyoak, T~~]]	+	[[Category: Balan MD]]
-	[[Category: ~~Johnson,~~ T A]]	+	[[Category: Holyoak T]]
-	[[Category: ~~Lotosky, W R~~]]	+	[[Category: Johnson TA]]
-	[[Category: ~~Mcleod, M J~~]]	+	[[Category: Lotosky WR]]
-	[[Category: ~~Gluconeogenesis]]~~	+	[[Category: Mcleod MJ]]
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Lyase~~]]	+

OCA at 08:47, 4 December 2019

OCA — Wed, 04 Dec 2019 08:47:41 GMT

←Older revision		Revision as of 08:47, 4 December 2019
Line 1:		Line 1:

	==Structure of rat cytosolic pepck in complex with 2,3-Pyridine dicarboxylic acid==		==Structure of rat cytosolic pepck in complex with 2,3-Pyridine dicarboxylic acid==
-	<StructureSection load='4ywd' size='340' side='right' caption='[[4ywd]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='4ywd' size='340' side='right'caption='[[4ywd]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ywd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YWD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ywd]] is a 1 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=4YWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YWD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wy8\|4wy8]], [[4wy9\|4wy9]], [[4wyb\|4wyb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wy8\|4wy8]], [[4wy9\|4wy9]], [[4wyb\|4wyb]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Pck1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] </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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [http://pdbe.org/4ywd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [http://www.ebi.ac.uk/pdbsum/4ywd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywd 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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [http://pdbe.org/4ywd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [http://www.ebi.ac.uk/pdbsum/4ywd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywd ProSAT]</span></td></tr>
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phosphoenolpyruvate carboxykinase 3D structures\|Phosphoenolpyruvate carboxykinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Balan, M D]]		[[Category: Balan, M D]]
	[[Category: Holyoak, T]]		[[Category: Holyoak, T]]

OCA at 15:56, 15 November 2017

OCA — Wed, 15 Nov 2017 15:56:14 GMT

←Older revision		Revision as of 15:56, 15 November 2017
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Phosphoenolpyruvate carboxykinase\|Phosphoenolpyruvate carboxykinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:38, 21 September 2017

OCA — Thu, 21 Sep 2017 04:38:24 GMT

←Older revision		Revision as of 04:38, 21 September 2017
Line 7:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wy8\|4wy8]], [[4wy9\|4wy9]], [[4wyb\|4wyb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wy8\|4wy8]], [[4wy9\|4wy9]], [[4wyb\|4wyb]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] </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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [http://pdbe.org/4ywd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [http://www.ebi.ac.uk/pdbsum/4ywd 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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [http://pdbe.org/4ywd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [http://www.ebi.ac.uk/pdbsum/4ywd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ywd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phosphoenolpyruvate carboxykinase\|Phosphoenolpyruvate carboxykinase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:44, 20 June 2016

OCA — Mon, 20 Jun 2016 07:44:55 GMT

←Older revision		Revision as of 07:44, 20 June 2016
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PCKGC_RAT PCKGC_RAT]] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.		[[http://www.uniprot.org/uniprot/PCKGC_RAT PCKGC_RAT]] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	For almost 40 years, it has been known that tryptophan metabolites and picolinic acid analogues act as inhibitors of gluconeogenesis. Early studies observed that 3-mercaptopicolinic acid (MPA) was a potent hypoglycemic agent via inhibition of glucose synthesis through the specific inhibition of phosphoenolpyruvate carboxykinase (PEPCK) in the gluconeogenesis pathway. Despite prior kinetic investigation, the mechanism of the inhibition by MPA is unclear. To clarify the mechanism of inhibition exerted by MPA on PEPCK, we have undertaken structural and kinetic studies. The kinetic data in concert with crystallographic structures of PEPCK in complex with MPA and the substrates for the reaction illustrate that PEPCK is inhibited by the binding of MPA at two discrete binding sites: one acting in a competitive fashion with PEP/OAA ( approximately 10 muM) and the other acting at a previously unidentified allosteric site (Ki approximately 150 muM). The structural studies suggest that binding of MPA to the allosteric pocket stabilizes an altered conformation of the nucleotide-binding site that in turn reduces the affinity of the enzyme for the nucleotide.
		+
		+	Inhibition and Allosteric Regulation of Monomeric Phosphoenolpyruvate Carboxykinase by 3-Mercaptopicolinic Acid.,Balan MD, Mcleod MJ, Lotosky WR, Ghaly M, Holyoak T Biochemistry. 2015 Sep 29;54(38):5878-87. doi: 10.1021/acs.biochem.5b00822. Epub , 2015 Sep 11. PMID:26322521<ref>PMID:26322521</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:17, 1 June 2016

OCA — Wed, 01 Jun 2016 08:17:50 GMT

←Older revision		Revision as of 08:17, 1 June 2016
Line 1:		Line 1:
		+
	==Structure of rat cytosolic pepck in complex with 2,3-Pyridine dicarboxylic acid==		==Structure of rat cytosolic pepck in complex with 2,3-Pyridine dicarboxylic acid==
	<StructureSection load='4ywd' size='340' side='right' caption='[[4ywd]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4ywd' size='340' side='right' caption='[[4ywd]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 10:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PCKGC_RAT PCKGC_RAT]] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.		[[http://www.uniprot.org/uniprot/PCKGC_RAT PCKGC_RAT]] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	For almost 40 years, it has been known that tryptophan metabolites and picolinic acid analogues act as inhibitors of gluconeogenesis. Early studies observed that 3-mercaptopicolinic acid (MPA) was a potent hypoglycemic agent via inhibition of glucose synthesis through the specific inhibition of phosphoenolpyruvate carboxykinase (PEPCK) in the gluconeogenesis pathway. Despite prior kinetic investigation, the mechanism of the inhibition by MPA is unclear. To clarify the mechanism of inhibition exerted by MPA on PEPCK, we have undertaken structural and kinetic studies. The kinetic data in concert with crystallographic structures of PEPCK in complex with MPA and the substrates for the reaction illustrate that PEPCK is inhibited by the binding of MPA at two discrete binding sites: one acting in a competitive fashion with PEP/OAA ( approximately 10 muM) and the other acting at a previously unidentified allosteric site (Ki approximately 150 muM). The structural studies suggest that binding of MPA to the allosteric pocket stabilizes an altered conformation of the nucleotide-binding site that in turn reduces the affinity of the enzyme for the nucleotide.
-
-	Inhibition and Allosteric Regulation of Monomeric Phosphoenolpyruvate Carboxykinase by 3-Mercaptopicolinic Acid.,Balan MD, Mcleod MJ, Lotosky WR, Ghaly M, Holyoak T Biochemistry. 2015 Sep 29;54(38):5878-87. doi: 10.1021/acs.biochem.5b00822. Epub , 2015 Sep 11. PMID:26322521<ref>PMID:26322521</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 20:55, 30 November 2015

OCA — Mon, 30 Nov 2015 20:55:45 GMT

←Older revision		Revision as of 20:55, 30 November 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Structure of rat cytosolic pepck in complex with 2,3-Pyridine dicarboxylic acid==
		+	<StructureSection load='4ywd' size='340' side='right' caption='[[4ywd]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ywd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YWD FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wy8\|4wy8]], [[4wy9\|4wy9]], [[4wyb\|4wyb]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] </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=4ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywd OCA], [http://pdbe.org/4ywd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ywd RCSB], [http://www.ebi.ac.uk/pdbsum/4ywd PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PCKGC_RAT PCKGC_RAT]] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	For almost 40 years, it has been known that tryptophan metabolites and picolinic acid analogues act as inhibitors of gluconeogenesis. Early studies observed that 3-mercaptopicolinic acid (MPA) was a potent hypoglycemic agent via inhibition of glucose synthesis through the specific inhibition of phosphoenolpyruvate carboxykinase (PEPCK) in the gluconeogenesis pathway. Despite prior kinetic investigation, the mechanism of the inhibition by MPA is unclear. To clarify the mechanism of inhibition exerted by MPA on PEPCK, we have undertaken structural and kinetic studies. The kinetic data in concert with crystallographic structures of PEPCK in complex with MPA and the substrates for the reaction illustrate that PEPCK is inhibited by the binding of MPA at two discrete binding sites: one acting in a competitive fashion with PEP/OAA ( approximately 10 muM) and the other acting at a previously unidentified allosteric site (Ki approximately 150 muM). The structural studies suggest that binding of MPA to the allosteric pocket stabilizes an altered conformation of the nucleotide-binding site that in turn reduces the affinity of the enzyme for the nucleotide.

-	~~The entry 4ywd is ON HOLD until Paper Publication~~	+	Inhibition and Allosteric Regulation of Monomeric Phosphoenolpyruvate Carboxykinase by 3-Mercaptopicolinic Acid.,Balan MD, Mcleod MJ, Lotosky WR, Ghaly M, Holyoak T Biochemistry. 2015 Sep 29;54(38):5878-87. doi: 10.1021/acs.biochem.5b00822. Epub , 2015 Sep 11. PMID:26322521<ref>PMID:26322521</ref>

-	~~Authors: Balan~~, M.D.~~, Johnson, T.A., Mcleod, M.J., Lotosky, W.R., Holyoak, T~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Structure of rat cytosolic pepck in complex with 2,3~~-~~Pyridine dicarboxylic acid~~	+	<div class="pdbe-citations 4ywd" style="background-color:#fffaf0;"></div>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	== References ==
-	~~[[Category: Mcleod, M.J]]~~	+	<references/>
-	~~[[Category: Johnson, T.A]]~~	+	__TOC__
-	[[Category: Balan, M.D]]	+	</StructureSection>
		+	[[Category: Balan, M D]]
	[[Category: Holyoak, T]]		[[Category: Holyoak, T]]
-	[[Category: Lotosky, W.R]]	+	[[Category: Johnson, T A]]
		+	[[Category: Lotosky, W R]]
		+	[[Category: Mcleod, M J]]
		+	[[Category: Gluconeogenesis]]
		+	[[Category: Kinase]]
		+	[[Category: Lyase]]

OCA at 11:15, 22 April 2015

OCA — Wed, 22 Apr 2015 11:15:00 GMT

←Older revision		Revision as of 11:15, 22 April 2015
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Balan, M.D., Johnson, T.A., Mcleod, M.J., Lotosky, W.R., Holyoak, T.		Authors: Balan, M.D., Johnson, T.A., Mcleod, M.J., Lotosky, W.R., Holyoak, T.

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

OCA — Wed, 01 Apr 2015 11:58:14 GMT

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

←Older revision

Revision as of 11:58, 1 April 2015