Acta Cryst. (2013). D69, 2008-2016 [ doi:10.1107/S0907444913017046 ]
Abstract: The first structure of a bacterial -phosphoglucomutase with an overall fold similar to eukaryotic phosphomannomutases is reported. Unlike most -phosphoglucomutases within the -D-phosphohexomutase superfamily, it belongs to subclass IIb of the haloacid dehalogenase superfamily (HADSF). It catalyzes the reversible conversion of -glucose 1-phosphate to glucose 6-phosphate. The crystal structure of -phosphoglucomutase from Lactococcus lactis (APGM) was determined at 1.5 Å resolution and contains a sulfate and a glycerol bound at the enzyme active site that partially mimic the substrate. A dimeric form of APGM is present in the crystal and in solution, an arrangement that may be functionally relevant. The catalytic mechanism of APGM and its strict specificity towards -glucose 1-phosphate are discussed.
PDB reference: 4bnd
Keywords: -phosphoglucomutases; haloacid dehalogenase superfamily; Lactococcus lactis; phosphomannomutases; -glucose 1-phosphate; eukaryotic phosphomannomutases; sugar metabolism.
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