4c4s - Revision history

OCA at 12:03, 20 December 2023

OCA — Wed, 20 Dec 2023 12:03:41 GMT

←Older revision		Revision as of 12:03, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c4s]] 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=4C4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4S FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c4s]] 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=4C4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4S FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</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]] 1.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [https://pdbe.org/4c4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [https://www.ebi.ac.uk/pdbsum/4c4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4s 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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [https://pdbe.org/4c4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [https://www.ebi.ac.uk/pdbsum/4c4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4s 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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	beta-Phosphoglucomutase (betaPGM) catalyzes isomerization of beta-d-glucose 1-phosphate (betaG1P) into d-glucose 6-phosphate (G6P) via sequential phosphoryl transfer steps using a beta-d-glucose 1,6-bisphosphate (betaG16BP) intermediate. Synthetic fluoromethylenephosphonate and methylenephosphonate analogs of betaG1P deliver novel step 1 transition state analog (TSA) complexes for betaPGM, incorporating trifluoromagnesate and tetrafluoroaluminate surrogates of the phosphoryl group. Within an invariant protein conformation, the beta-d-glucopyranose ring in the betaG1P TSA complexes (step 1) is flipped over and shifted relative to the G6P TSA complexes (step 2). Its equatorial hydroxyl groups are hydrogen-bonded directly to the enzyme rather than indirectly via water molecules as in step 2. The (C)O-P bond orientation for binding the phosphate in the inert phosphate site differs by approximately 30 degrees between steps 1 and 2. By contrast, the orientations for the axial O-Mg-O alignment for the TSA of the phosphoryl group in the catalytic site differ by only approximately 5 degrees , and the atoms representing the five phosphorus-bonded oxygens in the two transition states (TSs) are virtually superimposable. The conformation of betaG16BP in step 1 does not fit into the same invariant active site for step 2 by simple positional interchange of the phosphates: the TS alignment is achieved by conformational change of the hexose rather than the protein.
		+
		+	alpha-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction.,Jin Y, Bhattasali D, Pellegrini E, Forget SM, Baxter NJ, Cliff MJ, Bowler MW, Jakeman DL, Blackburn GM, Waltho JP Proc Natl Acad Sci U S A. 2014 Aug 7. pii: 201402850. PMID:25104750<ref>PMID:25104750</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c4s" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:26, 7 September 2022

OCA — Wed, 07 Sep 2022 17:26:57 GMT

←Older revision		Revision as of 17:26, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c4s' size='340' side='right'caption='[[4c4s]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='4c4s' size='340' side='right'caption='[[4c4s]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c4s]] 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=4C4S OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C4S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c4s]] 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=4C4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4S FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4r\|4c4r]], [[4c4t\|4c4t]]</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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [https://pdbe.org/4c4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [https://www.ebi.ac.uk/pdbsum/4c4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4s 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/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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [~~http~~://pdbe.org/4c4s PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c4s PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4s 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>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	beta-Phosphoglucomutase (betaPGM) catalyzes isomerization of beta-d-glucose 1-phosphate (betaG1P) into d-glucose 6-phosphate (G6P) via sequential phosphoryl transfer steps using a beta-d-glucose 1,6-bisphosphate (betaG16BP) intermediate. Synthetic fluoromethylenephosphonate and methylenephosphonate analogs of betaG1P deliver novel step 1 transition state analog (TSA) complexes for betaPGM, incorporating trifluoromagnesate and tetrafluoroaluminate surrogates of the phosphoryl group. Within an invariant protein conformation, the beta-d-glucopyranose ring in the betaG1P TSA complexes (step 1) is flipped over and shifted relative to the G6P TSA complexes (step 2). Its equatorial hydroxyl groups are hydrogen-bonded directly to the enzyme rather than indirectly via water molecules as in step 2. The (C)O-P bond orientation for binding the phosphate in the inert phosphate site differs by approximately 30 degrees between steps 1 and 2. By contrast, the orientations for the axial O-Mg-O alignment for the TSA of the phosphoryl group in the catalytic site differ by only approximately 5 degrees , and the atoms representing the five phosphorus-bonded oxygens in the two transition states (TSs) are virtually superimposable. The conformation of betaG16BP in step 1 does not fit into the same invariant active site for step 2 by simple positional interchange of the phosphates: the TS alignment is achieved by conformational change of the hexose rather than the protein.	+
-		+
-	alpha-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction.,Jin Y, Bhattasali D, Pellegrini E, Forget SM, Baxter NJ, Cliff MJ, Bowler MW, Jakeman DL, Blackburn GM, Waltho JP Proc Natl Acad Sci U S A. 2014 Aug 7. pii: 201402850. PMID:25104750<ref>PMID:25104750</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4c4s" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
-	*[[Beta-phosphoglucomutase\|Beta-phosphoglucomutase]]	+	*[[Beta-phosphoglucomutase 3D structures\|Beta-phosphoglucomutase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacterium~~ lactis ~~lister 1873]]~~	+	[[Category: Lactococcus lactis]]
-	~~[[Category: Beta-phosphoglucomutase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bowler~~, M W~~]]	+	[[Category: Bowler MW]]
-	[[Category: Pellegrini, E]]	+	[[Category: Pellegrini E]]
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Metal fluoride]]~~	+
-	~~[[Category: Mutase]]~~	+
-	~~[[Category: Phosphoryl transfer]]~~	+
-	~~[[Category: Transition state~~]]	+

OCA at 09:24, 20 March 2019

OCA — Wed, 20 Mar 2019 09:24:32 GMT

←Older revision		Revision as of 09:24, 20 March 2019
Line 1:		Line 1:

	==Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride==		==Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride==
-	<StructureSection load='4c4s' size='340' side='right' caption='[[4c4s]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='4c4s' size='340' side='right'caption='[[4c4s]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c4s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c4s]] 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=4C4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4S FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4r\|4c4r]], [[4c4t\|4c4t]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4r\|4c4r]], [[4c4t\|4c4t]]</td></tr>
Line 27:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacterium lactis lister 1873]]
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
		+	[[Category: Large Structures]]
	[[Category: Bowler, M W]]		[[Category: Bowler, M W]]
	[[Category: Pellegrini, E]]		[[Category: Pellegrini, E]]

OCA at 04:35, 5 August 2016

OCA — Fri, 05 Aug 2016 04:35:19 GMT

←Older revision		Revision as of 04:35, 5 August 2016
Line 1:		Line 1:
		+
	==Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride==		==Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride==
	<StructureSection load='4c4s' size='340' side='right' caption='[[4c4s]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='4c4s' size='340' side='right' caption='[[4c4s]], [[Resolution\|resolution]] 1.50Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4r\|4c4r]], [[4c4t\|4c4t]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4r\|4c4r]], [[4c4t\|4c4t]]</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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [http://www.ebi.ac.uk/pdbsum/4c4s 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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [http://pdbe.org/4c4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [http://www.ebi.ac.uk/pdbsum/4c4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4s ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4c4s" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 15:50, 25 December 2014

OCA — Thu, 25 Dec 2014 15:50:41 GMT

←Older revision		Revision as of 15:50, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c4s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4S FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c4s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4S FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4r\|4c4r]], [[4c4t\|4c4t]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4r\|4c4r]], [[4c4t\|4c4t]]</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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [http://www.ebi.ac.uk/pdbsum/4c4s 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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [http://www.ebi.ac.uk/pdbsum/4c4s 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
-	[[Category: Bowler, M W.]]	+	[[Category: Bowler, M W]]
-	[[Category: Pellegrini, E.]]	+	[[Category: Pellegrini, E]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Metal fluoride]]		[[Category: Metal fluoride]]

OCA at 13:20, 20 August 2014

OCA — Wed, 20 Aug 2014 13:20:16 GMT

←Older revision		Revision as of 13:20, 20 August 2014
Line 8:		Line 8:
	<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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [http://www.ebi.ac.uk/pdbsum/4c4s PDBsum]</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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [http://www.ebi.ac.uk/pdbsum/4c4s PDBsum]</span></td></tr>
	<table>		<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	beta-Phosphoglucomutase (betaPGM) catalyzes isomerization of beta-d-glucose 1-phosphate (betaG1P) into d-glucose 6-phosphate (G6P) via sequential phosphoryl transfer steps using a beta-d-glucose 1,6-bisphosphate (betaG16BP) intermediate. Synthetic fluoromethylenephosphonate and methylenephosphonate analogs of betaG1P deliver novel step 1 transition state analog (TSA) complexes for betaPGM, incorporating trifluoromagnesate and tetrafluoroaluminate surrogates of the phosphoryl group. Within an invariant protein conformation, the beta-d-glucopyranose ring in the betaG1P TSA complexes (step 1) is flipped over and shifted relative to the G6P TSA complexes (step 2). Its equatorial hydroxyl groups are hydrogen-bonded directly to the enzyme rather than indirectly via water molecules as in step 2. The (C)O-P bond orientation for binding the phosphate in the inert phosphate site differs by approximately 30 degrees between steps 1 and 2. By contrast, the orientations for the axial O-Mg-O alignment for the TSA of the phosphoryl group in the catalytic site differ by only approximately 5 degrees , and the atoms representing the five phosphorus-bonded oxygens in the two transition states (TSs) are virtually superimposable. The conformation of betaG16BP in step 1 does not fit into the same invariant active site for step 2 by simple positional interchange of the phosphates: the TS alignment is achieved by conformational change of the hexose rather than the protein.
		+
		+	alpha-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction.,Jin Y, Bhattasali D, Pellegrini E, Forget SM, Baxter NJ, Cliff MJ, Bowler MW, Jakeman DL, Blackburn GM, Waltho JP Proc Natl Acad Sci U S A. 2014 Aug 7. pii: 201402850. PMID:25104750<ref>PMID:25104750</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+
		+	==See Also==
		+	*[[Beta-phosphoglucomutase\|Beta-phosphoglucomutase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:25, 16 July 2014

OCA — Wed, 16 Jul 2014 10:25:24 GMT

←Older revision		Revision as of 10:25, 16 July 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	==Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride==
-		+	<StructureSection load='4c4s' size='340' side='right' caption='[[4c4s]], [[Resolution\|resolution]] 1.50Å' scene=''>
-	~~The entry 4c4s is ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4c4s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4S FirstGlance]. <br>
-	~~Authors: Pellegrini, E., Bowler, M.W.~~	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</scene><br>
-		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c4r\|4c4r]], [[4c4t\|4c4t]]</td></tr>
-	~~Description:~~ Structure of beta-phosphoglucomutase in complex with an alpha-fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride	+	<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=4c4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4s RCSB], [http://www.ebi.ac.uk/pdbsum/4c4s PDBsum]</span></td></tr>
		+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Beta-phosphoglucomutase]]
		+	[[Category: Bowler, M W.]]
		+	[[Category: Pellegrini, E.]]
		+	[[Category: Isomerase]]
		+	[[Category: Metal fluoride]]
		+	[[Category: Mutase]]
		+	[[Category: Phosphoryl transfer]]
		+	[[Category: Transition state]]

OCA at 07:29, 11 June 2014

OCA — Wed, 11 Jun 2014 07:29:58 GMT

←Older revision		Revision as of 07:29, 11 June 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c4s is ON HOLD	+	The entry 4c4s is ON HOLD until Paper Publication

	Authors: Pellegrini, E., Bowler, M.W.		Authors: Pellegrini, E., Bowler, M.W.

	Description: Structure of beta-phosphoglucomutase in complex with an alpha-fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride		Description: Structure of beta-phosphoglucomutase in complex with an alpha-fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride

OCA: Protected "4c4s" [edit=sysop:move=sysop]

OCA — Fri, 20 Sep 2013 03:18:06 GMT

Protected "4c4s" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:18, 20 September 2013

OCA: New page: '''Unreleased structure''' The entry 4c4s is ON HOLD Authors: Pellegrini, E., Bowler, M.W. Description: Structure of beta-phosphoglucomutase in complex with an alpha-fluorophosphonate ...

OCA — Fri, 20 Sep 2013 03:18:05 GMT

New page: '''Unreleased structure''' The entry 4c4s is ON HOLD Authors: Pellegrini, E., Bowler, M.W. Description: Structure of beta-phosphoglucomutase in complex with an alpha-fluorophosphonate ...

New page

'''Unreleased structure'''

The entry 4c4s is ON HOLD

Authors: Pellegrini, E., Bowler, M.W.

Description: Structure of beta-phosphoglucomutase in complex with an alpha-fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride