4BND

Structure of an atypical alpha-phosphoglucomutase similar to eukaryotic phosphomannomutases

Summary for 4BND

• Entry DOI: 10.2210/pdb4bnd/pdb
• Descriptor: ALPHA-PHOSPHOGLUCOMUTASE, GLYCEROL, SULFATE ION, ... (5 entities in total)
• Functional Keywords: isomerase, substrate specificity, phosphoglucose interconversion
• Biological source: LACTOCOCCUS LACTIS SUBSP. CREMORIS MG1363; More
• Total number of polymer chains: 2
• Total formula weight: 57544.91

Authors

Nogly, P.,Matias, P.M.,De Rosa, M.,Castro, R.,Santos, H.,Neves, A.R.,Archer, M. (deposition date: 2013-05-14, release date: 2013-10-02, Last modification date: 2024-05-08)

Primary citation

Nogly, P.,Matias, P.M.,De Rosa, M.,Castro, R.,Santos, H.,Neves, A.R.,Archer, M.
High-Resolution Structure of an Atypical [Alpha]-Phosphoglucomutase Related to Eukaryotic Phosphomannomutases
Acta Crystallogr.,Sect.D, 69:2008-, 2013

PubMed 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.

PubMed: 24100319
DOI: 10.1107/S0907444913017046

Experimental method

X-RAY DIFFRACTION (1.5 Å)