2FV1

UGL_D88N/dGlcA-GlcNAc

Summary for 2FV1

• Entry DOI: 10.2210/pdb2fv1/pdb
• Related: 2FUZ 2FV0
• Descriptor: Unsaturated glucuronyl hydrolase, 2,6-anhydro-3-deoxy-L-threo-hex-2-enonic acid-(1-3)-2-acetamido-2-deoxy-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: alpha6/alpha6-barrel, hydrolase
• Biological source: Bacillus sp.
• Cellular location: Cytoplasm: Q9RC92
• Total number of polymer chains: 2
• Total formula weight: 86553.37

Authors

Itoh, T.,Hashimoto, W.,Mikami, B.,Murata, K. (deposition date: 2006-01-28, release date: 2006-05-30, Last modification date: 2023-10-25)

Primary citation

Itoh, T.,Hashimoto, W.,Mikami, B.,Murata, K.
Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1
Biochem.Biophys.Res.Commun., 344:253-262, 2006

PubMed Abstract: Bacterial unsaturated glucuronyl hydrolases (UGLs) together with polysaccharide lyases are responsible for the complete depolymerization of mammalian extracellular matrix glycosaminoglycans. UGL acts on various oligosaccharides containing unsaturated glucuronic acid (DeltaGlcA) at the nonreducing terminus and releases DeltaGlcA through hydrolysis. In this study, we demonstrate the substrate recognition mechanism of the UGL of Bacillus sp. GL1 by determining the X-ray crystallographic structure of its substrate-enzyme complexes. The tetrasaccharide-enzyme complex demonstrated that at least four subsites are present in the active pocket. Although several amino acid residues are crucial for substrate binding, the enzyme strongly recognizes DeltaGlcA at subsite -1 through the formation of hydrogen bonds and stacking interactions, and prefers N-acetyl-d-galactosamine and glucose rather than N-acetyl-d-glucosamine as a residue accommodated in subsite +1, due to the steric hindrance.

PubMed: 16630576
DOI: 10.1016/j.bbrc.2006.03.141

Experimental method

X-RAY DIFFRACTION (1.73 Å)