1zol - Revision history

OCA at 07:12, 23 August 2023

OCA — Wed, 23 Aug 2023 07:12:04 GMT

←Older revision		Revision as of 07:12, 23 August 2023
Line 3:		Line 3:
	<StructureSection load='1zol' size='340' side='right'caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1zol' size='340' side='right'caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacterium_lactis"_lister_1873 "bacterium~~ lactis~~" lister 1873~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZOL FirstGlance]. <br>
-	</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>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.9Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;'>[[1o08\|1o08]]~~, [[~~1lvh~~\|~~1lvh]], [[1z4n\|1z4n]], [[1z4o\|1z4o~~]]~~</div>~~</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='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>LL0429 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1358~~ "~~Bacterium lactis~~" ~~Lister 1873])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6]~~ </~~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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [https://pdbe.org/1zol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [https://www.ebi.ac.uk/pdbsum/1zol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zol 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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [https://pdbe.org/1zol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [https://www.ebi.ac.uk/pdbsum/1zol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA]] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref>	+	[https://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacterium~~ lactis ~~lister 1873]]~~	+	[[Category: Lactococcus lactis]]
-	~~[[Category: Beta-phosphoglucomutase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Allen~~, K N~~]]	+	[[Category: Allen KN]]
-	[[Category: Dai, J]]	+	[[Category: Dai J]]
-	[[Category: Dunaway-Mariano, D]]	+	[[Category: Dunaway-Mariano D]]
-	[[Category: Tremblay~~, L W~~]]	+	[[Category: Tremblay LW]]
-	[[Category: Wang, L]]	+	[[Category: Wang L]]
-	[[Category: Zhang, G]]	+	[[Category: Zhang G]]
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Native beta-phosphoglucomutase~~]]	+

OCA at 08:13, 27 January 2021

OCA — Wed, 27 Jan 2021 08:13:59 GMT

←Older revision		Revision as of 08:13, 27 January 2021
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	==native beta-PGM==		==native beta-PGM==
-	<StructureSection load='1zol' size='340' side='right' caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1zol' size='340' side='right'caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1ZOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZOL 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" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o08\|1o08]], [[1lvh\|1lvh]], [[1z4n\|1z4n]], [[1z4o\|1z4o]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o08\|1o08]], [[1lvh\|1lvh]], [[1z4n\|1z4n]], [[1z4o\|1z4o]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [~~http~~://pdbe.org/1zol PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1zol PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1zol 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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [https://pdbe.org/1zol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [https://www.ebi.ac.uk/pdbsum/1zol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA]] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref>	+	[[https://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA]] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1zol" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1zol" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Beta-phosphoglucomutase 3D structures\|Beta-phosphoglucomutase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 40:
	[[Category: Bacterium lactis lister 1873]]		[[Category: Bacterium lactis lister 1873]]
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
		+	[[Category: Large Structures]]
	[[Category: Allen, K N]]		[[Category: Allen, K N]]
	[[Category: Dai, J]]		[[Category: Dai, J]]

OCA at 08:44, 2 May 2018

OCA — Wed, 02 May 2018 08:44:20 GMT

←Older revision		Revision as of 08:44, 2 May 2018
Line 1:		Line 1:
		+
	==native beta-PGM==		==native beta-PGM==
	<StructureSection load='1zol' size='340' side='right' caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1zol' size='340' side='right' caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [http://pdbe.org/1zol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [http://www.ebi.ac.uk/pdbsum/1zol 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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [http://pdbe.org/1zol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [http://www.ebi.ac.uk/pdbsum/1zol PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/1zol_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/1zol_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1zol" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1zol" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Beta-phosphoglucomutase\|Beta-phosphoglucomutase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:29, 9 February 2016

OCA — Tue, 09 Feb 2016 12:29:14 GMT

←Older revision		Revision as of 12:29, 9 February 2016
Line 19:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zol ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 22:15, 10 September 2015

OCA — Thu, 10 Sep 2015 22:15:44 GMT

←Older revision		Revision as of 22:15, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1zol' size='340' side='right' caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1zol' size='340' side='right' caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Lactococcus_lactis Lactococcus~~ lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZOL 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o08\|1o08]], [[1lvh\|1lvh]], [[1z4n\|1z4n]], [[1z4o\|1z4o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o08\|1o08]], [[1lvh\|1lvh]], [[1z4n\|1z4n]], [[1z4o\|1z4o]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 ~~Lactococcus~~ lactis])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [http://www.ebi.ac.uk/pdbsum/1zol 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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [http://pdbe.org/1zol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [http://www.ebi.ac.uk/pdbsum/1zol PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	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 1zol" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacterium lactis lister 1873]]
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
-	[[Category: Lactococcus lactis]]
	[[Category: Allen, K N]]		[[Category: Allen, K N]]
	[[Category: Dai, J]]		[[Category: Dai, J]]

OCA at 06:49, 25 December 2014

OCA — Thu, 25 Dec 2014 06:49:17 GMT

←Older revision		Revision as of 06:49, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZOL FirstGlance]. <br>		<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZOL FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><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><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o08\|1o08]], [[1lvh\|1lvh]], [[1z4n\|1z4n]], [[1z4o\|1z4o]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o08\|1o08]], [[1lvh\|1lvh]], [[1z4n\|1z4n]], [[1z4o\|1z4o]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [http://www.ebi.ac.uk/pdbsum/1zol 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=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [http://www.ebi.ac.uk/pdbsum/1zol PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA]] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
	[[Category: Lactococcus lactis]]		[[Category: Lactococcus lactis]]
-	[[Category: Allen, K N.]]	+	[[Category: Allen, K N]]
-	[[Category: Dai, J.]]	+	[[Category: Dai, J]]
-	[[Category: Dunaway-Mariano, D.]]	+	[[Category: Dunaway-Mariano, D]]
-	[[Category: Tremblay, L W.]]	+	[[Category: Tremblay, L W]]
-	[[Category: Wang, L.]]	+	[[Category: Wang, L]]
-	[[Category: Zhang, G.]]	+	[[Category: Zhang, G]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Native beta-phosphoglucomutase]]		[[Category: Native beta-phosphoglucomutase]]

OCA at 23:44, 29 September 2014

OCA — Mon, 29 Sep 2014 23:44:16 GMT

←Older revision		Revision as of 23:44, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1zol.~~png~~\|~~left~~\|200px]]	+	==native beta-PGM==
		+	<StructureSection load='1zol' size='340' side='right' caption='[[1zol]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1zol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZOL FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o08\|1o08]], [[1lvh\|1lvh]], [[1z4n\|1z4n]], [[1z4o\|1z4o]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LL0429 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zol RCSB], [http://www.ebi.ac.uk/pdbsum/1zol PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/1zol_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Lactococcus lactis beta-phosphoglucomutase (beta-PGM) catalyzes the interconversion of beta-d-glucose 1-phosphate (beta-G1P) and beta-d-glucose 6-phosphate (G6P), forming beta-d-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. Beta-PGM conserves the core domain catalytic scaffold of the phosphatase branch of the HAD (haloalkanoic acid dehalogenase) enzyme superfamily, yet it has evolved to function as a mutase rather than as a phosphatase. This work was carried out to identify the structural basis underlying this diversification of function. In this paper, we examine beta-PGM activation by the Mg(2+) cofactor, beta-PGM activation by Asp8 phosphorylation, and the role of cap domain closure in substrate discrimination. First, the 1.90 A resolution X-ray crystal structure of the Mg(2+)-beta-PGM complex is examined in the context of previously reported structures of the Mg(2+)-alpha-d-galactose-1-phosphate-beta-PGM, Mg(2+)-phospho-beta-PGM, and Mg(2+)-beta-glucose-6-phosphate-1-phosphorane-beta-PGM complexes to identify conformational changes that occur during catalytic turnover. The essential role of Asp8 in nucleophilic catalysis was confirmed by demonstrating that the D8A and D8E mutants are devoid of catalytic activity. Comparison of the ligands to Mg(2+) in the different complexes shows that a single Mg(2+) coordination site must alternatively accommodate water, phosphate, and the phosphorane intermediate during catalytic turnover. Limited involvement of the HAD family metal-binding loop in Mg(2+) anchoring in beta-PGM is consistent with the relatively loose binding indicated by the large K(m) for Mg(2+) activation (270 +/- 20 microM) and with the retention of activity found in the E169A/D170A double loop mutant. Comparison of the relative positions of cap and core domains in the different complexes indicated that interaction of cap domain Arg49 with the "nontransferring" phosphoryl group of the substrate ligand might stabilize the cap-closed conformation, as required for active site desolvation and alignment of Asp10 for acid-base catalysis. Kinetic analyses of the specificity of beta-PGM toward phosphoryl group donors and the specificity of phospho-beta-PGM toward phosphoryl group acceptors were carried out. The results support a substrate induced-fit mechanism of beta-PGM catalysis, which allows phosphomutase activity to dominate over the intrinsic phosphatase activity. Last, we present evidence that the autophosphorylation of beta-PGM by the substrate beta-G1P accounts for the origin of phospho-beta-PGM in the cell.

-	~~{{STRUCTURE_1zol\| PDB=1zol \| SCENE= }}~~	+	Catalytic cycling in beta-phosphoglucomutase: a kinetic and structural analysis.,Zhang G, Dai J, Wang L, Dunaway-Mariano D, Tremblay LW, Allen KN Biochemistry. 2005 Jul 12;44(27):9404-16. PMID:15996095<ref>PMID:15996095</ref>

-	~~===native beta-PGM===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_15996095}}~~	+	==See Also==
-		+	*[[Beta-phosphoglucomutase\|Beta-phosphoglucomutase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1zol~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:015996095<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
	[[Category: Lactococcus lactis]]		[[Category: Lactococcus lactis]]

OCA: Protected "1zol" [edit=sysop:move=sysop]

OCA — Sat, 05 Jan 2013 16:58:07 GMT

Protected "1zol" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:58, 5 January 2013

OCA at 16:58, 5 January 2013

OCA — Sat, 05 Jan 2013 16:58:05 GMT

←Older revision		Revision as of 16:58, 5 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1zol.png\|left\|200px]]		[[Image:1zol.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1zol", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1zol\| PDB=1zol \| SCENE= }}		{{STRUCTURE_1zol\| PDB=1zol \| SCENE= }}

	===native beta-PGM===		===native beta-PGM===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15996095}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15996095 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15996095}}		{{ABSTRACT_PUBMED_15996095}}

	==About this Structure==		==About this Structure==
-	~~1ZOL~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA].	+	[[1zol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15996095~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015996095</ref><references group="xtra"/>
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
	[[Category: Lactococcus lactis]]		[[Category: Lactococcus lactis]]
Line 32:		Line 20:
	[[Category: Wang, L.]]		[[Category: Wang, L.]]
	[[Category: Zhang, G.]]		[[Category: Zhang, G.]]
		+	[[Category: Isomerase]]
	[[Category: Native beta-phosphoglucomutase]]		[[Category: Native beta-phosphoglucomutase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:47:35 2009''

OCA at 07:47, 17 February 2009

OCA — Tue, 17 Feb 2009 07:47:37 GMT

←Older revision		Revision as of 07:47, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	1ZOL is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA].	+	1ZOL is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOL OCA].

	==Reference==		==Reference==
-	~~Catalytic cycling in beta-phosphoglucomutase: a kinetic and structural analysis., Zhang G, Dai J, Wang L, Dunaway-Mariano D, Tremblay LW, Allen KN, Biochemistry. 2005 Jul 12;44(27):9404-16.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/15996095 15996095]~~	+	<ref group="xtra">PMID:15996095</ref><references group="xtra"/>
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
	[[Category: Lactococcus lactis]]		[[Category: Lactococcus lactis]]
-	[[Category: Single protein]]
	[[Category: Allen, K N.]]		[[Category: Allen, K N.]]
	[[Category: Dai, J.]]		[[Category: Dai, J.]]
Line 35:		Line 34:
	[[Category: Native beta-phosphoglucomutase]]		[[Category: Native beta-phosphoglucomutase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 13~~:27:~~40 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:47:35 2009''