8K7Y

Crystal structure of GH146 beta-L-arabinofuranosidase Bll3HypBA1 (amino acids 380-1051), ligand-free form

8K7Y の概要

• エントリーDOI: 10.2210/pdb8k7y/pdb
• 分子名称: beta1,3-L-arabinofuranoside, ZINC ION (3 entities in total)
• 機能のキーワード: beta-l-arabinofuranosidase, hydrolase
• 由来する生物種: Bifidobacterium longum subsp. longum JCM 1217
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 150405.90

構造登録者

Maruyama, S.,Pan, L.,Miyake, M.,Fujita, K.,Fushinobu, S. (登録日: 2023-07-27, 公開日: 2024-02-21)

主引用文献

Fujita, K.,Tsunomachi, H.,Lixia, P.,Maruyama, S.,Miyake, M.,Dakeshita, A.,Kitahara, K.,Tanaka, K.,Ito, Y.,Ishiwata, A.,Fushinobu, S.
Bifidobacterial GH146 beta-L-arabinofuranosidase for the removal of beta 1,3-L-arabinofuranosides on plant glycans.
Appl.Microbiol.Biotechnol., 108:199-199, 2024

PubMed Abstract: L-Arabinofuranosides with β-linkages are present in several plant molecules, such as arabinogalactan proteins (AGPs), extensin, arabinan, and rhamnogalacturonan-II. We previously characterized a β-L-arabinofuranosidase from Bifidobacterium longum subsp. longum JCM 1217, Bll1HypBA1, which was found to belong to the glycoside hydrolase (GH) family 127. This strain encodes two GH127 genes and two GH146 genes. In the present study, we characterized a GH146 β-L-arabinofuranosidase, Bll3HypBA1 (BLLJ_1848), which was found to constitute a gene cluster with AGP-degrading enzymes. This recombinant enzyme degraded AGPs and arabinan, which contain Araf-β1,3-Araf structures. In addition, the recombinant enzyme hydrolyzed oligosaccharides containing Araf-β1,3-Araf structures but not those containing Araf-β1,2-Araf and Araf-β1,5-Araf structures. The crystal structures of Bll3HypBA1 were determined at resolutions up to 1.7 Å. The monomeric structure of Bll3HypBA1 comprised a catalytic (α/α) barrel and two β-sandwich domains. A hairpin structure with two β-strands was observed in Bll3HypBA1, to extend from a β-sandwich domain and partially cover the active site. The active site contains a Zn ion coordinated by Cys-Glu and exhibits structural conservation of the GH127 cysteine glycosidase Bll1HypBA1. This is the first study to report on a β1,3-specific β-L-arabinofuranosidase. KEY POINTS: • β1,3-l-Arabinofuranose residues are present in arabinogalactan proteins and arabinans as a terminal sugar. • β-l-Arabinofuranosidases are widely present in intestinal bacteria. • Bll3HypBA1 is the first enzyme characterized as a β1,3-linkage-specific β-l-arabinofuranosidase.

PubMed: 38324037
DOI: 10.1007/s00253-024-13014-8

実験手法

X-RAY DIFFRACTION (1.7 Å)