4D1J

The structure of the GH35 beta-galactosidase Bgl35A from Cellvibrio japonicas in complex with 1-Deoxygalactonojirimycin

4D1J の概要

• エントリーDOI: 10.2210/pdb4d1j/pdb
• 関連するPDBエントリー: 4D1I
• 分子名称: BETA-GALACTOSIDASE, PUTATIVE, BGL35A, (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, enzyme-carbohydrate interaction, glycosidase inhibition
• 由来する生物種: CELLVIBRIO JAPONICUS
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 489615.15

構造登録者

Larsbrink, J.,Thompson, A.J.,Lundqvist, M.,Gardner, J.G.,Davies, G.J.,Brumer, H. (登録日: 2014-05-02, 公開日: 2014-05-28, 最終更新日: 2023-12-20)

主引用文献

Larsbrink, J.,Thompson, A.J.,Lundqvist, M.,Gardner, J.G.,Davies, G.J.,Brumer, H.
A Complex Gene Locus Enables Xyloglucan Utilization in the Model Saprophyte Cellvibrio Japonicus.
Mol.Microbiol., 94:418-, 2014

PubMed Abstract: The degradation of plant biomass by saprophytes is an ecologically important part of the global carbon cycle, which has also inspired a vast diversity of industrial enzyme applications. The xyloglucans (XyGs) constitute a family of ubiquitous and abundant plant cell wall polysaccharides, yet the enzymology of XyG saccharification is poorly studied. Here, we present the identification and molecular characterization of a complex genetic locus that is required for xyloglucan utilization by the model saprophyte Cellvibrio japonicus. In harness, transcriptomics, reverse genetics, enzyme kinetics, and structural biology indicate that the encoded cohort of an α-xylosidase, a β-galactosidase, and an α-l-fucosidase is specifically adapted for efficient, concerted saccharification of dicot (fucogalacto)xyloglucan oligosaccharides following import into the periplasm via an associated TonB-dependent receptor. The data support a biological model of xyloglucan degradation by C. japonicus with striking similarities - and notable differences - to the complex polysaccharide utilization loci of the Bacteroidetes.

PubMed: 25171165
DOI: 10.1111/MMI.12776

実験手法

X-RAY DIFFRACTION (1.8 Å)