9UDY

Crystal structure of recombinant mushroom Agaricus bisporus mannose-binding protein with a longer C-terminal region

9UDY の概要

• エントリーDOI: 10.2210/pdb9udy/pdb
• 分子名称: Lectin-like fold protein, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• 機能のキーワード: lectin-like protein, agaricus bisporus, sugar binding protein
• 由来する生物種: Agaricus bisporus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18841.84

構造登録者

Yoshida, H.,Ismaya, W.T. (登録日: 2025-04-07, 公開日: 2025-05-21, 最終更新日: 2025-06-11)

主引用文献

Yoshida, H.,Nakakita, S.I.,Rachmawati, H.,Tjandrawinata, R.R.,Ismaya, W.T.
Crystal structure of a recombinant Agaricus bisporus mushroom mannose-binding protein with a longer C-terminal region.
Acta Crystallogr.,Sect.F, 81:241-248, 2025

PubMed Abstract: A lectin-like protein was discovered in Agaricus bisporus as part of the mushroom tyrosinase complex. The protein has a β-trefoil fold, which is typical of the ricin B-like-type lectin family. The structure of the recombinant protein has been elucidated, and its specific sugar-binding affinity towards mannose and mannitol has also been reported; therefore, the protein was named A. bisporus mannose-binding protein (Abmb). Although the sugar-binding site of Abmb is predicted to be close to the C-terminus, the sugar-binding site has not yet been determined. In this study, a variant of recombinant Abmb with a longer C-terminal region including a 6×His-tag was constructed and its structure was solved at 1.51 and 2.34 Å resolution in an orthorhombic and a monoclinic space group, respectively. The overall structure showed a β-trefoil fold as previously reported; however, several surface loop regions including the C-terminal region showed high flexibility. In addition, a glycan-search assay of this variant showed weak binding affinity towards β-D-galactose but no affinity towards α-D-mannose. The plasticity of the C-terminal tail could be related to the differences in the carbohydrate-binding affinity of Abmb.

PubMed: 40349189
DOI: 10.1107/S2053230X25003905

実験手法

X-RAY DIFFRACTION (1.51 Å)