5OLY

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

Summary for 5OLY

• Entry DOI: 10.2210/pdb5oly/pdb
• Descriptor: Beta-phosphoglucomutase, TRIFLUOROMAGNESATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: phosphoryl transfer, nmr labeling, 19f-nmr, isomerase
• Biological source: Lactococcus lactis subsp. lactis (Streptococcus lactis)
• Cellular location: Cytoplasm : P71447
• Total number of polymer chains: 2
• Total formula weight: 49331.25

Authors

Bowler, M.W.,von Velsen, J. (deposition date: 2017-07-28, release date: 2017-11-01, Last modification date: 2024-01-17)

Primary citation

Ampaw, A.,Carroll, M.,von Velsen, J.,Bhattasali, D.,Cohen, A.,Bowler, M.W.,Jakeman, D.L.
Observing enzyme ternary transition state analogue complexes by19F NMR spectroscopy.
Chem Sci, 8:8427-8434, 2017

PubMed Abstract: Ternary transition state analogue (TSA) complexes probing the isomerization of β-d-glucose 1-phosphate (G1P) into d-glucose 6-phosphate (G6P) catalyzed by catalytically active, fluorinated (5-fluorotryptophan), β-phosphoglucomutase (βPGM) have been observed directly by F NMR spectroscopy. In these complexes MgF and AlF are surrogates for the transferring phosphate. However, the relevance of these metal fluorides as TSA complexes has been queried. The 1D 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 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.

PubMed: 29619190
DOI: 10.1039/c7sc04204c

Experimental method

X-RAY DIFFRACTION (2 Å)