5H42

Crystal Structure of 1,2-beta-oligoglucan phosphorylase from Lachnoclostridium phytofermentans in complex with alpha-d-glucose-1-phosphate

5H42 の概要

• エントリーDOI: 10.2210/pdb5h42/pdb
• 関連するPDBエントリー: 5H3Z 5H40 5H41
• 分子名称: Uncharacterized protein, 1-O-phosphono-alpha-D-glucopyranose, alpha-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: beta-1, 2-glucan, glycoside phosphorylase, transferase
• 由来する生物種: Clostridium phytofermentans ISDg
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 256141.70

構造登録者

Nakajima, M.,Tanaka, N.,Furukawa, N.,Nihira, T.,Kodutsumi, Y.,Takahashi, Y.,Sugimoto, N.,Miyanaga, A.,Fushinobu, S.,Taguchi, H.,Nakai, H. (登録日: 2016-10-28, 公開日: 2017-03-01, 最終更新日: 2023-11-08)

主引用文献

Nakajima, M.,Tanaka, N.,Furukawa, N.,Nihira, T.,Kodutsumi, Y.,Takahashi, Y.,Sugimoto, N.,Miyanaga, A.,Fushinobu, S.,Taguchi, H.,Nakai, H.
Mechanistic insight into the substrate specificity of 1,2-beta-oligoglucan phosphorylase from Lachnoclostridium phytofermentans
Sci Rep, 7:42671-42671, 2017

PubMed Abstract: Glycoside phosphorylases catalyze the phosphorolysis of oligosaccharides into sugar phosphates. Recently, we found a novel phosphorylase acting on β-1,2-glucooligosaccharides with degrees of polymerization of 3 or more (1,2-β-oligoglucan phosphorylase, SOGP) in glycoside hydrolase family (GH) 94. Here, we characterized SOGP from Lachnoclostridium phytofermentans (LpSOGP) and determined its crystal structure. LpSOGP is a monomeric enzyme that contains a unique β-sandwich domain (Ndom1) at its N-terminus. Unlike the dimeric GH94 enzymes possessing catalytic pockets at their dimer interface, LpSOGP has a catalytic pocket between Ndom1 and the catalytic domain. In the complex structure of LpSOGP with sophorose, sophorose binds at subsites +1 to +2. Notably, the Glc moiety at subsite +1 is flipped compared with the corresponding ligands in other GH94 enzymes. This inversion suggests the great distortion of the glycosidic bond between subsites -1 and +1, which is likely unfavorable for substrate binding. Compensation for this disadvantage at subsite +2 can be accounted for by the small distortion of the glycosidic bond in the sophorose molecule. Therefore, the binding mode at subsites +1 and +2 defines the substrate specificity of LpSOGP, which provides mechanistic insights into the substrate specificity of a phosphorylase acting on β-1,2-glucooligosaccharides.

PubMed: 28198470
DOI: 10.1038/srep42671

実験手法

X-RAY DIFFRACTION (2.1 Å)