6S04

Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with N-glycolylneuraminic acid

6S04 の概要

• エントリーDOI: 10.2210/pdb6s04/pdb
• 関連するPDBエントリー: 6RZD 6S00
• 分子名称: exosialidase from uncultured bacterium pG7, ACETATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: (beta/alpha )8 barrel, hydrolase, sialidase, inverting, homodimer
• 由来する生物種: uncultured bacterium pG7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 119953.86

構造登録者

Bule, P.,Blagova, E.,Chuzel, L.,Taron, C.H.,Davies, G.J. (登録日: 2019-06-13, 公開日: 2019-11-06, 最終更新日: 2024-10-09)

主引用文献

Bule, P.,Chuzel, L.,Blagova, E.,Wu, L.,Gray, M.A.,Henrissat, B.,Rapp, E.,Bertozzi, C.R.,Taron, C.H.,Davies, G.J.
Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action.
Nat Commun, 10:4816-4816, 2019

PubMed Abstract: Sialic acids are a family of related sugars that play essential roles in many biological events intimately linked to cellular recognition in both health and disease. Sialidases are therefore orchestrators of cellular biology and important therapeutic targets for viral infection. Here, we sought to define if uncharacterized sialidases would provide distinct paradigms in sialic acid biochemistry. We show that a recently discovered sialidase family, whose first member EnvSia156 was isolated from hot spring metagenomes, defines an unusual structural fold and active centre constellation, not previously described in sialidases. Consistent with an inverting mechanism, EnvSia156 reveals a His/Asp active center in which the His acts as a Brønsted acid and Asp as a Brønsted base in a single-displacement mechanism. A predominantly hydrophobic aglycone site facilitates accommodation of a variety of 2-linked sialosides; a versatility that offers the potential for glycan hydrolysis across a range of biological and technological platforms.

PubMed: 31645552
DOI: 10.1038/s41467-019-12684-7

実験手法

X-RAY DIFFRACTION (2 Å)