9EP6

Alpha-Galactosaminidase family GH114 from Fusarium solani

9EP6 の概要

• エントリーDOI: 10.2210/pdb9ep6/pdb
• 関連するPDBエントリー: 9EP5 9EUX 9EUZ
• 分子名称: alpha-galactosidase, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: family gh114, galactosaminogalactan degradation, gag, hydrolase
• 由来する生物種: Fusarium solani
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 100292.75

構造登録者

Roth, C.,Moroz, O.V.,Miranda, S.A.D.,Jahn, L.,Blagova, E.,Lebedev, A.A.,Segura, D.R.,Stringer, M.A.,Friis, E.P.,Davies, G.J.,Wilson, K.S. (登録日: 2024-03-17, 公開日: 2025-04-23, 最終更新日: 2025-05-14)

主引用文献

Roth, C.,Moroz, O.V.,Miranda, S.A.D.,Jahn, L.,Blagova, E.V.,Lebedev, A.A.,Segura, D.R.,Stringer, M.A.,Friis, E.P.,Franco Cairo, J.P.L.,Davies, G.J.,Wilson, K.S.
Structures of alpha-galactosaminidases from the CAZy GH114 family and homologs defining a new GH191 family of glycosidases.
Acta Crystallogr D Struct Biol, 81:234-251, 2025

PubMed Abstract: Endo-galactosaminidases are an underexplored family of enzymes involved in the degradation of galactosaminogalactan (GAG) and other galactosamine-containing cationic exopolysaccharides produced by fungi and bacteria. These exopolysaccharides are part of the cell wall and extracellular matrix of microbial communities. Currently, these galactosaminidases are found in three distinct CAZy families: GH114, GH135 and GH166. Despite the widespread occurrence of these enzymes in nearly all bacterial and fungal clades, only limited biochemical and structural data are available for these three groups. To expand our knowledge of endo-galactosaminidases, we selected several sequences predicted to encode endo-galactosaminidases and produced them recombinantly for structural and functional studies. Only very few predicted proteins could be produced in soluble form, and activity against bacterial Pel (pellicle) polysaccharide could only be confirmed for one enzyme. Here, we report the structures of two bacterial and one fungal enzyme. Whereas the fungal enzyme belongs to family GH114, the two bacterial enzymes do not lie in the current GH families but instead define a new family, GH191. During structure solution we realized that crystals of all three enzymes had various defects including twinning and partial disorder, which in the case of a more severe pathology in one of the structures required the design of a specialized refinement/model-building protocol. Comparison of the structures revealed several features that might be responsible for the described activity pattern and substrate specificity compared with other GAG-degrading enzymes.

PubMed: 40232846
DOI: 10.1107/S2059798325002864

実験手法

X-RAY DIFFRACTION (1.61 Å)