Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.7/468
Título: High-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutases
Autor: Nogly, Przemyslaw
Matias, Pedro M.
de Rosa, Matteo
Castro, Rute
Santos, Helena
Neves, Ana Rute
Archer, Margarida
Palavras-chave: α-phosphoglucomutases
haloacid dehalogenase superfamily
Lactococcus lactis
α-glucose 1-phosphate
eukaryotic phosphomannomutases
sugar metabolism
Data: Out-2013
Editora: Wiley-Blackwell
Resumo: 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.
Peer review: yes
URI: http://hdl.handle.net/10400.7/468
DOI: 10.1107/S0907444913017046
Versão do Editor: http://journals.iucr.org/d/issues/2013/10/00/dz5291/index.html
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