6ER2

Ruminococcus gnavus IT-sialidase CBM40

6ER2 の概要

• エントリーDOI: 10.2210/pdb6er2/pdb
• 分子名称: BNR/Asp-box repeat protein (2 entities in total)
• 機能のキーワード: sialidase, cbm, sialic acid, sugar binding protein
• 由来する生物種: Ruminococcus gnavus ATCC 29149
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41011.89

構造登録者

Owen, C.D.,Tailford, L.E.,Taylor, G.L.,Juge, N. (登録日: 2017-10-16, 公開日: 2018-05-02, 最終更新日: 2024-01-17)

主引用文献

Owen, C.D.,Tailford, L.E.,Monaco, S.,Suligoj, T.,Vaux, L.,Lallement, R.,Khedri, Z.,Yu, H.,Lecointe, K.,Walshaw, J.,Tribolo, S.,Horrex, M.,Bell, A.,Chen, X.,Taylor, G.L.,Varki, A.,Angulo, J.,Juge, N.
Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus.
Nat Commun, 8:2196-2196, 2017

PubMed Abstract: Ruminococcus gnavus is a human gut symbiont wherein the ability to degrade mucins is mediated by an intramolecular trans-sialidase (RgNanH). RgNanH comprises a GH33 catalytic domain and a sialic acid-binding carbohydrate-binding module (CBM40). Here we used glycan arrays, STD NMR, X-ray crystallography, mutagenesis and binding assays to determine the structure and function of RgNanH_CBM40 (RgCBM40). RgCBM40 displays the canonical CBM40 β-sandwich fold and broad specificity towards sialoglycans with millimolar binding affinity towards α2,3- or α2,6-sialyllactose. RgCBM40 binds to mucus produced by goblet cells and to purified mucins, providing direct evidence for a CBM40 as a novel bacterial mucus adhesin. Bioinformatics data show that RgCBM40 canonical type domains are widespread among Firmicutes. Furthermore, binding of R. gnavus ATCC 29149 to intestinal mucus is sialic acid mediated. Together, this study reveals novel features of CBMs which may contribute to the biogeography of symbiotic bacteria in the gut.

PubMed: 29259165
DOI: 10.1038/s41467-017-02109-8

実験手法

X-RAY DIFFRACTION (1.73 Å)