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PDBsum entry 2fv0
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References listed in PDB file
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Key reference
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Title
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Substrate recognition by unsaturated glucuronyl hydrolase from bacillus sp. Gl1.
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Authors
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T.Itoh,
W.Hashimoto,
B.Mikami,
K.Murata.
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Ref.
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Biochem Biophys Res Commun, 2006,
344,
253-262.
[DOI no: ]
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PubMed id
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Abstract
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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.
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