View source for 5olx


==5-fluorotryptophan labeled beta-phosphoglucomutase in a closed conformation, orthorhomic crystal form==
<StructureSection load='5olx' size='340' side='right'caption='[[5olx]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5olx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis Lactococcus lactis subsp. lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OLX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=FTR:FLUOROTRYPTOPHANE'>FTR</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=5olx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5olx OCA], [https://pdbe.org/5olx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5olx RCSB], [https://www.ebi.ac.uk/pdbsum/5olx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5olx ProSAT]</span></td></tr>
</table>
== 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> 
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== 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<ref>PMID:29619190</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5olx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-phosphoglucomutase 3D structures|Beta-phosphoglucomutase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Lactococcus lactis subsp. lactis]]
[[Category: Large Structures]]
[[Category: Bowler MW]]
[[Category: Von Velsen J]]