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2whe

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==STRUCTURE OF NATIVE BETA-PHOSPHOGLUCOMUTASE IN AN OPEN CONFORMATION WITHOUT BOUND LIGANDS.==
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<StructureSection load='2whe' size='340' side='right' caption='[[2whe]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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==Structure of native Beta-Phosphoglucomutase in an open conformation without bound ligands.==
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<StructureSection load='2whe' size='340' side='right'caption='[[2whe]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2whe]] 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=2WHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WHE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2whe]] 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=2WHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WHE FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wf8|2wf8]], [[1z4n|1z4n]], [[2wf7|2wf7]], [[2wf9|2wf9]], [[1z4o|1z4o]], [[1o03|1o03]], [[2wf6|2wf6]], [[2wf5|2wf5]], [[2wfa|2wfa]], [[1zol|1zol]], [[1o08|1o08]], [[1lvh|1lvh]]</td></tr>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2whe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2whe OCA], [https://pdbe.org/2whe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2whe RCSB], [https://www.ebi.ac.uk/pdbsum/2whe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2whe ProSAT]</span></td></tr>
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<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=2whe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2whe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2whe RCSB], [http://www.ebi.ac.uk/pdbsum/2whe PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wh/2whe_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wh/2whe_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>
</jmolCheckbox>
</jmolCheckbox>
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</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].
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</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=2whe ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2whe" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Beta-phosphoglucomutase|Beta-phosphoglucomutase]]
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*[[Beta-phosphoglucomutase 3D structures|Beta-phosphoglucomutase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Beta-phosphoglucomutase]]
 
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
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[[Category: Alizadeh, T]]
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[[Category: Large Structures]]
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[[Category: Baxter, N J]]
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[[Category: Alizadeh T]]
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[[Category: Bermel, W]]
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[[Category: Baxter NJ]]
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[[Category: Blackburn, G M]]
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[[Category: Bermel W]]
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[[Category: Bowler, M W]]
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[[Category: Blackburn GM]]
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[[Category: Cliff, M J]]
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[[Category: Bowler MW]]
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[[Category: Hollfelder, F]]
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[[Category: Cliff MJ]]
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[[Category: Hounslow, A M]]
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[[Category: Hollfelder F]]
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[[Category: Pollard, S]]
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[[Category: Hounslow AM]]
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[[Category: Waltho, J P]]
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[[Category: Pollard S]]
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[[Category: Webster, C E]]
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[[Category: Waltho JP]]
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[[Category: Williams, N H]]
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[[Category: Webster CE]]
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[[Category: Haloacid dehalogenase superfamily]]
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[[Category: Williams NH]]
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[[Category: Isomerase]]
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[[Category: Phosphotransferase]]
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Current revision

Structure of native Beta-Phosphoglucomutase in an open conformation without bound ligands.

PDB ID 2whe

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