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

• Autor(a) principal: Nogly, Przemyslaw
• Data de Publicação: 2013
• Outros Autores: Matias, Pedro M., de Rosa, Matteo, Castro, Rute, Santos, Helena, Neves, Ana Rute, Archer, Margarida
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
• Texto Completo: http://hdl.handle.net/10400.7/468
• topic: α-phosphoglucomutases; haloacid dehalogenase superfamily; Lactococcus lactis; phosphomannomutases; α-glucose 1-phosphate; eukaryotic phosphomannomutases; sugar metabolism

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.