4bnd

Publication Abstract from PubMed

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 A 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.

High-resolution structure of an atypical alpha-phosphoglucomutase related to eukaryotic phosphomannomutases.,Nogly P, Matias PM, de Rosa M, Castro R, Santos H, Neves AR, Archer M Acta Crystallogr D Biol Crystallogr. 2013 Oct 1;69(Pt 10):2008-2016. Epub 2013, Sep 20. PMID:24100319^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.