6FIG

Crystal structure of the ANX1 ectodomain from Arabidopsis thaliana

Summary for 6FIG

• Entry DOI: 10.2210/pdb6fig/pdb
• Descriptor: 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)
• Functional Keywords: receptor kinase, malectin-like domain, membrane protein, arabidopsis thaliana, plant protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 95717.61

Authors

Santiago, J. (deposition date: 2018-01-18, release date: 2018-07-11, Last modification date: 2024-11-13)

Primary citation

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

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: 29968676
DOI: 10.1107/S205979831800774X

Experimental method

X-RAY DIFFRACTION (1.48 Å)