4OZO

Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG

4OZO の概要

• エントリーDOI: 10.2210/pdb4ozo/pdb
• 関連するPDBエントリー: 4OUE
• 分子名称: Putative lipoprotein, GLYCEROL, 2-nitrophenyl 1-thio-beta-D-galactopyranoside, ... (4 entities in total)
• 機能のキーワード: beta sandwich, glycosyl hydrolase gh29, hydrolase
• 由来する生物種: Bacteroides thetaiotaomicron
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107839.35

構造登録者

Lafite, P.,Daniellou, R.,Guillotin, L. (登録日: 2014-02-17, 公開日: 2014-03-05, 最終更新日: 2023-09-27)

主引用文献

Guillotin, L.,Lafite, P.,Daniellou, R.
Unraveling the substrate recognition mechanism and specificity of the unusual glycosyl hydrolase family 29 BT2192 from Bacteroides thetaiotaomicron.
Biochemistry, 53:1447-1455, 2014

PubMed Abstract: Glycosyl hydrolase (GH) family 29 (CAZy database) consists of retaining α-l-fucosidases. We have identified BT2192, a protein from Bacteroides thetaiotaomicron, as the first GH29 representative exhibiting both weak α-l-fucosidase and β-d-galactosidase activities. Determination and analysis of X-ray structures of BT2192 in complex with β-d-galactoside competitive inhibitors showed a new binding mode different from that of known GH29 enzymes. Three point mutations, specific to BT2192, prevent the canonical GH29 substrate α-l-fucose from binding efficiently to the fucosidase-like active site relative to other GH29 enzymes. β-d-Galactoside analogues bind and interact in a second pocket, which is not visible in other reported GH29 structures. Molecular simulations helped in the assessment of the flexibility of both substrates in their respective pocket. Hydrolysis of the fucosyl moiety from the putative natural substrates like 3-fucosyllactose or Lewis(X) antigen would be mainly due to the efficient interactions with the galactosyl moiety, in the second binding site, located more than 6-7 Å apart.

PubMed: 24527659
DOI: 10.1021/bi400951q

実験手法

X-RAY DIFFRACTION (2.6 Å)