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 1.514;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.
High-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutases / P. Nogly, P.M. Matias, M. de Rosa, R. Castro, H. Santos, A.R. Neves, M. Archer. - In: ACTA CRYSTALLOGRAPHICA. SECTION D, BIOLOGICAL CRYSTALLOGRAPHY. - ISSN 0907-4449. - 69:10(2013 Oct), pp. 2008-2016.
|Titolo:||High-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutases|
|Parole Chiave:||-glucose 1-phosphate; -phosphoglucomutases; eukaryotic phosphomannomutases; haloacid dehalogenase superfamily; Lactococcus lactis; phosphomannomutases; sugar metabolism|
|Settore Scientifico Disciplinare:||Settore BIO/10 - Biochimica|
|Data di pubblicazione:||ott-2013|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1107/S0907444913017046|
|Appare nelle tipologie:||01 - Articolo su periodico|