2FV0

UGL_D88N/dGlcA-Glc-Rha-Glc

2FV0 の概要

• エントリーDOI: 10.2210/pdb2fv0/pdb
• 関連するPDBエントリー: 2FUZ 2FV1
• 分子名称: Unsaturated glucuronyl hydrolase, 2,6-anhydro-3-deoxy-L-threo-hex-2-enonic acid-(1-4)-beta-D-glucopyranose-(1-4)-alpha-L-rhamnopyranose-(1-3)-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: alpha6/alpha6-barrel, hydrolase
• 由来する生物種: Bacillus sp.
• 細胞内の位置: Cytoplasm: Q9RC92
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86457.28

構造登録者

Itoh, T.,Hashimoto, W.,Mikami, B.,Murata, K. (登録日: 2006-01-28, 公開日: 2006-05-30, 最終更新日: 2024-12-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.91 Å)