Acta Crystallographica Section D

Biological Crystallography

Volume 69, Part 10 (October 2013)

research papers

Acta Cryst. (2013). D69, 2008-2016    [ doi:10.1107/S0907444913017046 ]

High-resolution structure of an atypical [alpha]-phosphoglucomutase related to eukaryotic phosphomannomutases

P. Nogly, P. M. Matias, M. de Rosa, R. Castro, H. Santos, A. R. Neves and M. Archer

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

PDB reference: 4bnd

Keywords: [alpha]-phosphoglucomutases; haloacid dehalogenase superfamily; Lactococcus lactis; phosphomannomutases; [alpha]-glucose 1-phosphate; eukaryotic phosphomannomutases; sugar metabolism.

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