High-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutases

Nogly, Przemyslaw; Matias, Pedro M.; de Rosa, Matteo; Castro, Rute; Santos, Helena; Neves, Ana Rute; Archer, Margarida

http://hdl.handle.net/10400.7/468

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Abstract(s)

The first structure of a bacterial α-phosphoglucomutase with an overall fold similar to eukaryotic phosphomannomutases is reported. Unlike most α-phosphoglucomutases within the α-D-phosphohexomutase superfamily, it belongs to subclass IIb of the haloacid dehalogenase superfamily (HADSF). It catalyzes the reversible conversion of α-glucose 1-phosphate to glucose 6-phosphate. The crystal structure of α-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 α-glucose 1-phosphate are discussed.

Keywords

α-phosphoglucomutases haloacid dehalogenase superfamily Lactococcus lactis phosphomannomutases α-glucose 1-phosphate eukaryotic phosphomannomutases sugar metabolism