6cfu - Revision history

OCA at 15:03, 4 October 2023

OCA — Wed, 04 Oct 2023 15:03:55 GMT

←Older revision		Revision as of 15:03, 4 October 2023
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	<StructureSection load='6cfu' size='340' side='right'caption='[[6cfu]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='6cfu' size='340' side='right'caption='[[6cfu]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6cfu]] 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=6CFU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6CFU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6cfu]] 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=6CFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CFU FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.244Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">PMM1, PMMH22 ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[http://en.wikipedia.org/wiki/Phosphomannomutase Phosphomannomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.8 5.4.2.8]~~ </~~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=6cfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cfu OCA], [https://pdbe.org/6cfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cfu RCSB], [https://www.ebi.ac.uk/pdbsum/6cfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cfu 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=6cfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cfu OCA], [~~http~~://pdbe.org/6cfu PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6cfu RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6cfu PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6cfu ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PMM1_HUMAN PMM1_HUMAN]] Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.	+	[https://www.uniprot.org/uniprot/PMM1_HUMAN PMM1_HUMAN] Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.
	<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: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Phosphomannomutase]]~~	+	[[Category: Allen KN]]
-	[[Category: Allen~~, K N~~]]	+	[[Category: Dunaway-Mariano D]]
-	[[Category: Dunaway-Mariano, D]]	+	[[Category: Ji T]]
-	[[Category: Ji, T]]	+
-	~~[[Category: Haloalkanoate dehalogenase superfamily]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Mutase]]~~	+
-	~~[[Category: Phosphatase~~]]	+

OCA at 08:25, 27 November 2019

OCA — Wed, 27 Nov 2019 08:25:30 GMT

←Older revision		Revision as of 08:25, 27 November 2019
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	==Structure of Human alpha-Phosphomannomutase 1 containing mutations R180K and R183K==		==Structure of Human alpha-Phosphomannomutase 1 containing mutations R180K and R183K==
-	<StructureSection load='6cfu' size='340' side='right' caption='[[6cfu]], [[Resolution\|resolution]] 2.24Å' scene=''>	+	<StructureSection load='6cfu' size='340' side='right'caption='[[6cfu]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6cfu]] 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=6CFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CFU FirstGlance]. <br>		<table><tr><td colspan='2'>[[6cfu]] 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=6CFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CFU FirstGlance]. <br>
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 6cfu" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6cfu" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Phosphomannomutase\|Phosphomannomutase]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Phosphomannomutase]]		[[Category: Phosphomannomutase]]
	[[Category: Allen, K N]]		[[Category: Allen, K N]]

OCA at 07:45, 23 May 2018

OCA — Wed, 23 May 2018 07:45:33 GMT

←Older revision		Revision as of 07:45, 23 May 2018
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	<StructureSection load='6cfu' size='340' side='right' caption='[[6cfu]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='6cfu' size='340' side='right' caption='[[6cfu]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6cfu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CFU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6cfu]] 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=6CFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CFU FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PMM1, PMMH22 ([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/Phosphomannomutase Phosphomannomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.8 5.4.2.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphomannomutase Phosphomannomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.8 5.4.2.8] </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=6cfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cfu OCA], [http://pdbe.org/6cfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cfu RCSB], [http://www.ebi.ac.uk/pdbsum/6cfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cfu 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=6cfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cfu OCA], [http://pdbe.org/6cfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cfu RCSB], [http://www.ebi.ac.uk/pdbsum/6cfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cfu ProSAT]</span></td></tr>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Phosphomannomutase]]		[[Category: Phosphomannomutase]]
	[[Category: Allen, K N]]		[[Category: Allen, K N]]

OCA at 06:17, 9 May 2018

OCA — Wed, 09 May 2018 06:17:48 GMT

←Older revision		Revision as of 06:17, 9 May 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6cfu is ~~ON HOLD until Paper~~ Publication	+	==Structure of Human alpha-Phosphomannomutase 1 containing mutations R180K and R183K==
		+	<StructureSection load='6cfu' size='340' side='right' caption='[[6cfu]], [[Resolution\|resolution]] 2.24Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6cfu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CFU FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphomannomutase Phosphomannomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.8 5.4.2.8] </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=6cfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cfu OCA], [http://pdbe.org/6cfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cfu RCSB], [http://www.ebi.ac.uk/pdbsum/6cfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cfu ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PMM1_HUMAN PMM1_HUMAN]] Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The human phosphomannomutases PMM1 and PMM2 catalyze the interconversion of hexose 6-phosphates and hexose 1-phosphates. The two isoforms share 66% sequence identity and have similar kinetic properties as mutases in vitro, but differ in their functional roles in vivo. Though the physiological role of PMM2 is catalysis of the mutase reaction that provides the mannose 1-phosphate (Man-1-P) essential for protein glycosylation, PMM1 is thought to provide a phosphohydrolase activity in the presence of inosine monophosphate (IMP), converting glucose 1,6-bisphosphate (Glu-1,6-P2) to glucose 6-phosphate (Glu-6-P), rescuing glycolysis during brain ischemia. To uncover the structural basis of how IMP binding converts PMM1 from a mutase to a phosphatase, the 1.93 A resolution structure of PMM1 complexed with IMP was determined. The structure reveals IMP bound at the substrate recruitment site, thus inhibiting the mutase activity while simultaneous activating a phosphatase activity (IMP Kact = 1.5 muM) resulting from the hydrolysis of the phospho-enzyme. The bound structure and site-directed mutagenesis confirm that the long-range electrostatic interactions provided by Arg180 and Arg183 conserved in PMM1 are the major contributors to IMP binding, and their oblation removes phosphatase but not mutase activity. These residues are not present in the PMM2 isoform, which consequently lacks significant phosphatase activity in the presence of IMP. T2 relaxation NMR and SAXS together support the hypothesis that IMP binding to PMM1 favors an enzyme conformation that is catalytically competent for water attack at the phosphoaspartyl intermediate. Such a mechanism may be generalizable to other enzymes that act through covalent intermediates.

-	~~Authors: Ji~~, T., Dunaway-Mariano, D., Allen~~, K~~.N.	+	The structural basis of the molecular switch between phosphatase and mutase functions of human phosphomannomutase 1 under ischemic conditions.,Ji T, Zhang C, Zheng L, Dunaway-Mariano D, Allen KN Biochemistry. 2018 Apr 25. doi: 10.1021/acs.biochem.8b00223. PMID:29695157<ref>PMID:29695157</ref>

-	~~Description: Structure~~ of ~~Human alpha~~-~~Phosphomannomutase 1 containing mutations R180K and R183K~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: Ji, T]]	+	<div class="pdbe-citations 6cfu" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Phosphomannomutase]]
		+	[[Category: Allen, K N]]
	[[Category: Dunaway-Mariano, D]]		[[Category: Dunaway-Mariano, D]]
-	[[Category: ~~Allen~~, ~~K.N~~]]	+	[[Category: Ji, T]]
		+	[[Category: Haloalkanoate dehalogenase superfamily]]
		+	[[Category: Isomerase]]
		+	[[Category: Mutase]]
		+	[[Category: Phosphatase]]

OCA at 06:06, 21 March 2018

OCA — Wed, 21 Mar 2018 06:06:02 GMT

←Older revision		Revision as of 06:06, 21 March 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6cfu is ON HOLD	+	The entry 6cfu is ON HOLD until Paper Publication

	Authors: Ji, T., Dunaway-Mariano, D., Allen, K.N.		Authors: Ji, T., Dunaway-Mariano, D., Allen, K.N.

OCA: Protected "6cfu" [edit=sysop:move=sysop]

OCA — Wed, 28 Feb 2018 05:02:10 GMT

Protected "6cfu" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:02, 28 February 2018

OCA: New page: '''Unreleased structure''' The entry 6cfu is ON HOLD Authors: Ji, T., Dunaway-Mariano, D., Allen, K.N. Description: Structure of Human alpha-Phosphomannomutase 1 containing mutations R...

OCA — Wed, 28 Feb 2018 05:02:09 GMT

New page: '''Unreleased structure''' The entry 6cfu is ON HOLD Authors: Ji, T., Dunaway-Mariano, D., Allen, K.N. Description: Structure of Human alpha-Phosphomannomutase 1 containing mutations R...

New page

'''Unreleased structure'''

The entry 6cfu is ON HOLD

Authors: Ji, T., Dunaway-Mariano, D., Allen, K.N.

Description: Structure of Human alpha-Phosphomannomutase 1 containing mutations R180K and R183K
[[Category: Unreleased Structures]]
[[Category: Ji, T]]
[[Category: Dunaway-Mariano, D]]
[[Category: Allen, K.N]]