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| | ==5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation== | | ==5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation== |
| - | <StructureSection load='5olw' size='340' side='right' caption='[[5olw]], [[Resolution|resolution]] 2.28Å' scene=''> | + | <StructureSection load='5olw' size='340' side='right'caption='[[5olw]], [[Resolution|resolution]] 2.28Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5olw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacla Lacla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OLW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OLW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5olw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_Il1403 Lactococcus lactis subsp. lactis Il1403]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OLW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.28Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pgmB, LL0429, L0001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272623 LACLA])</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=5olw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5olw OCA], [https://pdbe.org/5olw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5olw RCSB], [https://www.ebi.ac.uk/pdbsum/5olw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5olw 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=5olw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5olw OCA], [http://pdbe.org/5olw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5olw RCSB], [http://www.ebi.ac.uk/pdbsum/5olw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5olw 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==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: Beta-phosphoglucomutase]] | + | [[Category: Lactococcus lactis subsp. lactis Il1403]] |
| - | [[Category: Lacla]] | + | [[Category: Large Structures]] |
| - | [[Category: Bowler, M W]] | + | [[Category: Bowler MW]] |
| - | [[Category: Velsen, J von]] | + | [[Category: Von Velsen J]] |
| - | [[Category: 19f-nmr]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Nmr labeling]]
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| - | [[Category: Phosphoryl transfer]]
| + | |
| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
Ternary transition state analogue (TSA) complexes probing the isomerization of beta-d-glucose 1-phosphate (G1P) into d-glucose 6-phosphate (G6P) catalyzed by catalytically active, fluorinated (5-fluorotryptophan), beta-phosphoglucomutase (betaPGM) have been observed directly by (19)F NMR spectroscopy. In these complexes MgF3(-) and AlF4(-) are surrogates for the transferring phosphate. However, the relevance of these metal fluorides as TSA complexes has been queried. The 1D (19)F spectrum of a ternary TSA complex presented a molar equivalence between fluorinated enzyme, metal fluoride and non-isomerizable fluoromethylenephosphonate substrate analogue. Ring flips of the 5-fluoroindole ring remote from the active site were observed by both (19)F NMR and X-ray crystallography, but did not perturb function. This data unequivocally demonstrates that the concentration of the metal fluoride complexes is equivalent to the concentration of enzyme and ligand in the TSA complex in aqueous solution.
Observing enzyme ternary transition state analogue complexes by (19)F NMR spectroscopy.,Ampaw A, Carroll M, von Velsen J, Bhattasali D, Cohen A, Bowler MW, Jakeman DL Chem Sci. 2017 Dec 1;8(12):8427-8434. doi: 10.1039/c7sc04204c. Epub 2017 Oct 23. PMID:29619190[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Qian N, Stanley GA, Bunte A, Radstrom P. Product formation and phosphoglucomutase activities in Lactococcus lactis: cloning and characterization of a novel phosphoglucomutase gene. Microbiology. 1997 Mar;143 ( Pt 3):855-65. PMID:9084169
- ↑ Lahiri SD, Zhang G, Dai J, Dunaway-Mariano D, Allen KN. Analysis of the substrate specificity loop of the HAD superfamily cap domain. Biochemistry. 2004 Mar 16;43(10):2812-20. PMID:15005616 doi:10.1021/bi0356810
- ↑ Ampaw A, Carroll M, von Velsen J, Bhattasali D, Cohen A, Bowler MW, Jakeman DL. Observing enzyme ternary transition state analogue complexes by (19)F NMR spectroscopy. Chem Sci. 2017 Dec 1;8(12):8427-8434. doi: 10.1039/c7sc04204c. Epub 2017 Oct 23. PMID:29619190 doi:http://dx.doi.org/10.1039/c7sc04204c
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