6FIG
Crystal structure of the ANX1 ectodomain from Arabidopsis thaliana
6FIG の概要
エントリーDOI | 10.2210/pdb6fig/pdb |
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-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
機能のキーワード | receptor kinase, malectin-like domain, membrane protein, arabidopsis thaliana, plant protein |
由来する生物種 | Arabidopsis thaliana (thale cress) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 95717.61 |
構造登録者 | |
主引用文献 | Moussu, S.,Augustin, S.,Roman, A.O.,Broyart, C.,Santiago, J. Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction. Acta Crystallogr D Struct Biol, 74:671-680, 2018 Cited by PubMed Abstract: Complex cell-to-cell communication between the male pollen tube and the female reproductive organs is required for plant fertilization. A family of Catharanthus roseus receptor kinase 1-like (CrRLK1L) membrane receptors has been genetically implicated in this process. Here, crystal structures of the CrRLK1Ls ANXUR1 and ANXUR2 are reported at 1.48 and 1.1 Å resolution, respectively. The structures reveal a novel arrangement of two malectin-like domains connected by a short β-hairpin linker and stabilized by calcium ions. The canonical carbohydrate-interaction surfaces of related animal and bacterial carbohydrate-binding modules are not conserved in plant CrRLK1Ls. In line with this, the binding of chemically diverse oligosaccharides to ANXUR1 and HERCULES1 could not be detected. Instead, CrRLK1Ls have evolved a protein-protein interface between their malectin domains which forms a deep cleft lined by highly conserved aromatic and polar residues. Analysis of the glycosylation patterns of different CrRLK1Ls and their oligomeric states suggests that this cleft could resemble a binding site for a ligand required for receptor activation of CrRLK1Ls. PubMed: 29968676DOI: 10.1107/S205979831800774X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.48 Å) |
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