5k55 - Revision history

OCA at 10:39, 27 September 2023

2023-09-27T10:39:54Z

←Older revision		Revision as of 10:39, 27 September 2023
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	==Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state in complex with fructose-6-phosphate==		==Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state in complex with fructose-6-phosphate==
-	<StructureSection load='5k55' size='340' side='right' caption='[[5k55]], [[Resolution\|resolution]] 1.98Å' scene=''>	+	<StructureSection load='5k55' size='340' side='right'caption='[[5k55]], [[Resolution\|resolution]] 1.98Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k55]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K55 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5K55 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k55]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K55 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</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]] 1.977Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ifa\|3ifa]]~~, [[~~3ifc~~\|~~3ifc]], [[4he0\|4he0]], [[4he1\|4he1]], [[4he2\|4he2]], [[5et5\|5et5]], [[5et6\|5et6]], [[5et7\|5et7]], [[5et8\|5et8~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>FBP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=9606 HUMAN])</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=5k55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k55 OCA], [https://pdbe.org/5k55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k55 RCSB], [https://www.ebi.ac.uk/pdbsum/5k55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k55 ProSAT]</span></td></tr>
-	~~<tr id='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[http~~:~~//en.wikipedia.org/wiki/Fructose~~-~~bisphosphatase Fructose~~-~~bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11]~~ </~~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=5k55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k55 OCA], [~~http~~://pdbe.org/5k55 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5k55 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5k55 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5k55 ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/F16P2_HUMAN F16P2_HUMAN]
-	~~Human fructose-1,6-bisphosphatase is an allosteric enzyme that is regulated by different ligands. There are only two known isozymes in human tissues~~: the liver isozyme (the key enzyme of gluconeogenesis), which is regulated by fructose 2,6-bisphosphate, and its muscle counterpart (participating in glycogen synthesis), which is regulated by calcium ions. AMP, which is an allosteric inhibitor of both isozymes, inhibits the muscle isozyme with an I(0.5) that is 35-100 times lower than for the liver isozyme and the reason for this difference remains obscure. In studies aiming at an explanation of the main differences in the regulation of the two isozymes, it has been shown that only one residue, in position 69, regulates the sensitivity towards calcium ions. As a consequence of this finding, an E69Q mutant of the muscle isozyme, which is insensitive to calcium ions while retaining all other kinetic properties resembling the liver isozyme, has been prepared and crystallized. Here, two crystal structures of this mutant enzyme in complex with AMP with and without fructose 6-phosphate (the product of the catalytic reaction) are presented. The AMP binding pattern of the muscle isozyme is quite similar to that of the liver isozyme and the T conformations of the two isozymes are nearly the same.	+
-		+
-	Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.,Zarzycki M, Kolodziejczyk R, Maciaszczyk-Dziubinska E, Wysocki R, Jaskolski M, Dzugaj A Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1028-34. doi:, 10.1107/~~S090744491104385X. Epub 2011 Nov 18. PMID:22120740<ref>PMID:22120740<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 5k55" style="background-color:#fffaf0;"><~~/~~div>~~	+

	==See Also==		==See Also==
-	*[[Fructose-1%2C6-bisphosphatase\|Fructose-1%2C6-bisphosphatase]]	+	*[[Fructose-1%2C6-bisphosphatase 3D structures\|Fructose-1%2C6-bisphosphatase 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Fructose-bisphosphatase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Barciszewski, J]]	+	[[Category: Barciszewski J]]
-	[[Category: Dzugaj, A]]	+	[[Category: Dzugaj A]]
-	[[Category: Jaskolski, M]]	+	[[Category: Jaskolski M]]
-	[[Category: Kolodziejczyk, R]]	+	[[Category: Kolodziejczyk R]]
-	[[Category: Rakus, D]]	+	[[Category: Rakus D]]
-	[[Category: Wisniewski, J]]	+	[[Category: Wisniewski J]]
-	~~[[Category: Carbohydrate metabolism]]~~	+
-	~~[[Category: E69q mutant]]~~	+
-	~~[[Category: F6p]]~~	+
-	~~[[Category: Fbpase]]~~	+
-	~~[[Category: Glyconeogenesis]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Leucine lock]]~~	+
-	~~[[Category: Muscle izozyme]]~~	+
-	~~[[Category: R-state~~]]	+

OCA at 22:01, 9 August 2018

2018-08-09T22:01:57Z

←Older revision		Revision as of 22:01, 9 August 2018
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5k55" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5k55" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Fructose-1%2C6-bisphosphatase\|Fructose-1%2C6-bisphosphatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:44, 16 November 2017

2017-11-16T10:44:27Z

←Older revision		Revision as of 10:44, 16 November 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5k55 is ~~ON HOLD until Paper~~ Publication	+	==Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state in complex with fructose-6-phosphate==
		+	<StructureSection load='5k55' size='340' side='right' caption='[[5k55]], [[Resolution\|resolution]] 1.98Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5k55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K55 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ifa\|3ifa]], [[3ifc\|3ifc]], [[4he0\|4he0]], [[4he1\|4he1]], [[4he2\|4he2]], [[5et5\|5et5]], [[5et6\|5et6]], [[5et7\|5et7]], [[5et8\|5et8]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FBP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] </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=5k55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k55 OCA], [http://pdbe.org/5k55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k55 RCSB], [http://www.ebi.ac.uk/pdbsum/5k55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k55 ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human fructose-1,6-bisphosphatase is an allosteric enzyme that is regulated by different ligands. There are only two known isozymes in human tissues: the liver isozyme (the key enzyme of gluconeogenesis), which is regulated by fructose 2,6-bisphosphate, and its muscle counterpart (participating in glycogen synthesis), which is regulated by calcium ions. AMP, which is an allosteric inhibitor of both isozymes, inhibits the muscle isozyme with an I(0.5) that is 35-100 times lower than for the liver isozyme and the reason for this difference remains obscure. In studies aiming at an explanation of the main differences in the regulation of the two isozymes, it has been shown that only one residue, in position 69, regulates the sensitivity towards calcium ions. As a consequence of this finding, an E69Q mutant of the muscle isozyme, which is insensitive to calcium ions while retaining all other kinetic properties resembling the liver isozyme, has been prepared and crystallized. Here, two crystal structures of this mutant enzyme in complex with AMP with and without fructose 6-phosphate (the product of the catalytic reaction) are presented. The AMP binding pattern of the muscle isozyme is quite similar to that of the liver isozyme and the T conformations of the two isozymes are nearly the same.

-	~~Authors: Barciszewski~~, J., ~~Wisniewski, J.~~, Kolodziejczyk, R., ~~Dzugaj~~, A., Jaskolski, M~~., Rakus~~, D.	+	Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.,Zarzycki M, Kolodziejczyk R, Maciaszczyk-Dziubinska E, Wysocki R, Jaskolski M, Dzugaj A Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1028-34. doi:, 10.1107/S090744491104385X. Epub 2011 Nov 18. PMID:22120740<ref>PMID:22120740</ref>

-	~~Description: Human muscle fructose-1~~,6-~~bisphosphatase E69Q mutant in active R~~-~~state in complex with fructose-6-phosphate~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: ~~Rakus, D~~]]	+	<div class="pdbe-citations 5k55" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Fructose-bisphosphatase]]
		+	[[Category: Human]]
	[[Category: Barciszewski, J]]		[[Category: Barciszewski, J]]
	[[Category: Dzugaj, A]]		[[Category: Dzugaj, A]]
-	[[Category: Wisniewski, J]]
	[[Category: Jaskolski, M]]		[[Category: Jaskolski, M]]
	[[Category: Kolodziejczyk, R]]		[[Category: Kolodziejczyk, R]]
		+	[[Category: Rakus, D]]
		+	[[Category: Wisniewski, J]]
		+	[[Category: Carbohydrate metabolism]]
		+	[[Category: E69q mutant]]
		+	[[Category: F6p]]
		+	[[Category: Fbpase]]
		+	[[Category: Glyconeogenesis]]
		+	[[Category: Hydrolase]]
		+	[[Category: Leucine lock]]
		+	[[Category: Muscle izozyme]]
		+	[[Category: R-state]]

OCA at 10:10, 9 March 2017

2017-03-09T10:10:44Z

←Older revision		Revision as of 10:10, 9 March 2017
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	Description: Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state in complex with fructose-6-phosphate		Description: Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state in complex with fructose-6-phosphate
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Dzugaj, A]]
-	[[Category: Wisniewski, J]]
	[[Category: Rakus, D]]		[[Category: Rakus, D]]
	[[Category: Barciszewski, J]]		[[Category: Barciszewski, J]]
		+	[[Category: Dzugaj, A]]
		+	[[Category: Wisniewski, J]]
	[[Category: Jaskolski, M]]		[[Category: Jaskolski, M]]
	[[Category: Kolodziejczyk, R]]		[[Category: Kolodziejczyk, R]]

OCA at 00:01, 13 July 2016

2016-07-13T00:01:13Z

←Older revision		Revision as of 00:01, 13 July 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5k55 is ON HOLD	+	The entry 5k55 is ON HOLD until Paper Publication

	Authors: Barciszewski, J., Wisniewski, J., Kolodziejczyk, R., Dzugaj, A., Jaskolski, M., Rakus, D.		Authors: Barciszewski, J., Wisniewski, J., Kolodziejczyk, R., Dzugaj, A., Jaskolski, M., Rakus, D.

OCA: Protected "5k55" [edit=sysop:move=sysop]

2016-06-01T14:20:33Z

Protected "5k55" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:20, 1 June 2016

OCA: New page: '''Unreleased structure''' The entry 5k55 is ON HOLD Authors: Barciszewski, J., Wisniewski, J., Kolodziejczyk, R., Dzugaj, A., Jaskolski, M., Rakus, D. Description: Human muscle fructo...

2016-06-01T14:20:27Z

New page: '''Unreleased structure''' The entry 5k55 is ON HOLD Authors: Barciszewski, J., Wisniewski, J., Kolodziejczyk, R., Dzugaj, A., Jaskolski, M., Rakus, D. Description: Human muscle fructo...

New page

'''Unreleased structure'''

The entry 5k55 is ON HOLD

Authors: Barciszewski, J., Wisniewski, J., Kolodziejczyk, R., Dzugaj, A., Jaskolski, M., Rakus, D.

Description: Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state in complex with fructose-6-phosphate
[[Category: Unreleased Structures]]
[[Category: Dzugaj, A]]
[[Category: Wisniewski, J]]
[[Category: Rakus, D]]
[[Category: Barciszewski, J]]
[[Category: Jaskolski, M]]
[[Category: Kolodziejczyk, R]]