5Y96

Crystal structure of ANXUR1 extracellular domain from Arabidopsis thaliana

5Y96 の概要

• エントリーDOI: 10.2210/pdb5y96/pdb
• 関連するPDBエントリー: 5Y92
• 分子名称: Receptor-like protein kinase ANXUR1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: receptor-like kinase, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : Q9SR05 Q9SR05
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87498.61

構造登録者

Du, S.,Xiao, J.Y. (登録日: 2017-08-22, 公開日: 2018-02-28, 最終更新日: 2024-11-06)

主引用文献

Du, S.,Qu, L.J.,Xiao, J.
Crystal structures of the extracellular domains of the CrRLK1L receptor-like kinases ANXUR1 and ANXUR2
Protein Sci., 27:886-892, 2018

PubMed Abstract: Catharanthus roseus Receptor-Like Kinase 1-like (CrRLK1L) proteins contain two tandem malectin-like modules in their extracellular domains (ECDs) and function in diverse signaling pathways in plants. Malectin is a carbohydrate-binding protein in animals and recognizes a number of diglucosides; however, it remains unclear how the two malectin-like domains in the CrRLK1L proteins sense the ligand molecule. In this study, we reveal the crystal structures of the ECDs of ANXUR1 and ANXUR2, two CrRLK1L members in Arabidopsis thaliana that have critical functions in controlling pollen tube rupture during the fertilization process. We show that the two malectin-like domains in these proteins pack together to form a rigid architecture. Unlike animal malectin, these malectin-like domains lack residues involved in binding to the diglucosides, suggesting that they have a distinct ligand-binding mechanism. A cleft is observed between the two malectin-like domains, which might function as a potential ligand-binding pocket.

PubMed: 29388293
DOI: 10.1002/pro.3381

実験手法

X-RAY DIFFRACTION (1.8 Å)