5OAW

Crystal structure of Aspergillus fumigatus N-acetylphosphoglucosamine mutase in complex with GlcNAc-6P and magnesium

Summary for 5OAW

• Entry DOI: 10.2210/pdb5oaw/pdb
• Descriptor: Phosphoacetylglucosamine mutase, MAGNESIUM ION, 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: mutase, n-acetylphosphoglucosamine, aspergillus fumigatus, isomerase
• Biological source: Aspergillus lentulus
• Total number of polymer chains: 2
• Total formula weight: 120920.82

Authors

Raimi, O.G.,Hurtado-Guerrero, R. (deposition date: 2017-06-24, release date: 2018-07-11, Last modification date: 2024-10-23)

Primary citation

Raimi, O.G.,Hurtado-Guerrero, R.,van Aalten, D.M.F.
Evidence for substrate-assisted catalysis inN-acetylphosphoglucosamine mutase.
Biochem. J., 475:2547-2557, 2018

PubMed Abstract: -acetylphosphoglucosamine mutase (AGM1) is a key component of the hexosamine biosynthetic pathway that produces UDP-GlcNAc, an essential precursor for a wide range of glycans in eukaryotes. AGM belongs to the α-d-phosphohexomutase metalloenzyme superfamily and catalyzes the interconversion of -acetylglucosamine-6-phosphate (GlcNAc-6P) to -acetylglucosamine-1-phosphate (GlcNAc-1P) through -acetylglucosamine-1,6-bisphosphate (GlcNAc-1,6-bisP) as the catalytic intermediate. Although there is an understanding of the phosphoserine-dependent catalytic mechanism at enzymatic and structural level, the identity of the requisite catalytic base in AGM1/phosphoglucomutases is as yet unknown. Here, we present crystal structures of a Michaelis complex of AGM1 with GlcNAc-6P and Mg, and a complex of the inactive Ser69Ala mutant together with glucose-1,6-bisphosphate (Glc-1,6-bisP) that represents key snapshots along the reaction co-ordinate. Together with mutagenesis, these structures reveal that the phosphate group of the hexose-1,6-bisP intermediate may act as the catalytic base.

PubMed: 29967067
DOI: 10.1042/BCJ20180172

Experimental method

X-RAY DIFFRACTION (2.34 Å)