High‐resolution structure of an atypical α‐phosphoglucomutase related to eukaryotic phosphomannomutases. (8th October 2013)

• Record Type: Journal Article
• Authors: Nogly, Przemyslaw; Matias, Pedro M.; de Rosa, Matteo; Castro, Rute; Santos, Helena; Neves, Ana Rute; Archer, Margarida
• Is Part Of: Acta crystallographica. Volume 69:Part 10(2013:Oct.)
• Page Start: 2008
• Page End: 2016
• Publication Date: 2013-10-08
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S0907444913017046
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Lactococcus lactis</italic> (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.</p> </abstract>