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

DOI: 10.1107/S0907444913017046 DOI Help

Authors: Przemyslaw Nogly (Universidade Nova de Lisboa (ITQB–UNL)) , Pedro M. Matias (Institudo Tecnologia Quimica e Biologica) , Matteo De Rosa (Instituto Gulbenkian de Ciência (IGC)) , Rute Castro (Universidade Nova de Lisboa (ITQB–UNL)) , Helena Santos (Universidade Nova de Lisboa (ITQB–UNL)) , Ana Rute Neves (Universidade Nova de Lisboa (ITQB–UNL)) , Margarida Archer (Universidade Nova de Lisboa (ITQB–UNL))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Biological Crystallography , VOL 69 , PAGES 2008 - 2016

State: Published (Approved)
Published: October 2013

Abstract: 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.

Journal Keywords: α-phosphoglucomutases; haloacid dehalogenase superfamily; Lactococcus lactis; phosphomannomutases; α-glucose 1-phosphate; eukaryotic phosphomannomutases; sugar metabolism

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-Macromolecular Crystallography