5olx | pdb_00005olx

5-fluorotryptophan labeled beta-phosphoglucomutase in a closed conformation, orthorhomic crystal form

spinqualitylabelsall models 5olx, resolution 1.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5olx is a 1 chain structure with sequence from "lactococcus_lactis_subsp._diacitilactis_(sic)"_(garvie_and_farrow_1982)_schleifer_et_al._1986 "lactococcus lactis subsp. diacitilactis (sic)" (garvie and farrow 1982) schleifer et al. 1986. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BG6, MG, MGF NonStd Res: FTR Gene: pgmB, LL0429, L0001 ("Lactococcus lactis subsp. diacitilactis (sic)" (Garvie and Farrow 1982) Schleifer et al. 1986) Activity: Beta-phosphoglucomutase, with EC number 5.4.2.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-phosphoglucomutase

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