7YAQ
Phloem lectin (PP2)C34S mutant
7YAQ の概要
| エントリーDOI | 10.2210/pdb7yaq/pdb |
| 関連するPDBエントリー | 7VS6 7VUB 7VWB 7W4B |
| 分子名称 | 17 kDa phloem lectin (2 entities in total) |
| 機能のキーワード | phloem lectin, chitin-binding lectin, sugar binding protein |
| 由来する生物種 | Cucumis sativus (cucumber) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 17623.81 |
| 構造登録者 | Sivaji, N.,Bobbili, K.B.,Priya, B.,Suguna, K.,Surolia, A. (登録日: 2022-06-28, 公開日: 2023-03-08, 最終更新日: 2024-05-08) |
| 主引用文献 | Bobbili, K.B.,Sivaji, N.,Priya, B.,Suguna, K.,Surolia, A. Structure and interactions of the phloem lectin (phloem protein 2) Cus17 from Cucumis sativus. Structure, 31:464-, 2023 Cited by PubMed Abstract: Phloem protein 2 (PP2) contributes crucially to phloem-based defense in plants by binding to carbohydrates displayed by pathogens. However, its three-dimensional structure and the sugar binding site remained unexplored. Here, we report the crystal structure of the dimeric PP2 Cus17 from Cucumis sativus in its apo form and complexed with nitrobenzene, N-acetyllactosamine, and chitotriose. Each protomer of Cus17 consists of two antiparallel four-stranded twisted β sheets, a β hairpin, and three short helices forming a β sandwich architectural fold. This structural fold has not been previously observed in other plant lectin families. Structure analysis of the lectin-carbohydrate complexes reveals an extended carbohydrate binding site in Cus17, composed mostly of aromatic amino acids. Our studies suggest a highly conserved tertiary structure and a versatile binding site capable of recognizing motifs common to diverse glycans on plant pathogens/pests, which makes the PP2 family suited for phloem-based plant defense. PubMed: 36882058DOI: 10.1016/j.str.2023.02.008 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.853 Å) |
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