3ZKK

Structure of the xylo-oligosaccharide specific solute binding protein from Bifidobacterium animalis subsp. lactis Bl-04 in complex with xylotetraose

3ZKK の概要

• エントリーDOI: 10.2210/pdb3zkk/pdb
• 関連するPDBエントリー: 3ZKL 4C1T 4C1U
• 分子名称: XOS BINDING PROTEIN, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL, ... (4 entities in total)
• 機能のキーワード: transport protein, probiotic, prebiotic, abc transport
• 由来する生物種: BIFIDOBACTERIUM ANIMALIS SUBSP. LACTIS BL-04
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45205.40

構造登録者

Ejby, M.,Vujicic-Zagar, A.,Fredslund, F.,Svensson, B.,Slotboom, D.J.,Abou Hachem, M. (登録日: 2013-01-23, 公開日: 2013-10-30, 最終更新日: 2024-10-23)

主引用文献

Ejby, M.,Fredslund, F.,Vujicic-Zagar, A.,Svensson, B.,Slotboom, D.J.,Abou Hachem, M.
Structural Basis for Arabinoxylo-Oligosaccharide Capture by the Probiotic Bifidobacterium Animalis Subsp. Lactis Bl-04
Mol.Microbiol., 90:1100-, 2013

PubMed Abstract: Glycan utilization plays a key role in modulating the composition of the gut microbiota, but molecular insight into oligosaccharide uptake by this microbial community is lacking. Arabinoxylo-oligosaccharides (AXOS) are abundant in the diet, and are selectively fermented by probiotic bifidobacteria in the colon. Here we show how selectivity for AXOS uptake is established by the probiotic strain Bifidobacterium animalis subsp. lactis Bl-04. The binding protein BlAXBP, which is associated with an ATP-binding cassette (ABC) transporter that mediates the uptake of AXOS, displays an exceptionally broad specificity for arabinosyl-decorated and undecorated xylo-oligosaccharides, with preference for tri- and tetra-saccharides. Crystal structures of BlAXBP in complex with four different ligands revealed the basis for this versatility. Uniquely, the protein was able to recognize oligosaccharides in two opposite orientations, which facilitates the optimization of interactions with the various ligands. Broad substrate specificity was further enhanced by a spacious binding pocket accommodating decorations at different mainchain positions and conformational flexibility of a lid-like loop. Phylogenetic and genetic analyses show that BlAXBP is highly conserved within Bifidobacterium, but is lacking in other gut microbiota members. These data indicate niche adaptation within Bifidobacterium and highlight the metabolic syntrophy (cross-feeding) among the gut microbiota.

PubMed: 24279727
DOI: 10.1111/MMI.12419

実験手法

X-RAY DIFFRACTION (2.198 Å)