Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction
| Autor: | Steven Moussu, Sebastian Augustin, Caroline Broyart, Andra Octavia Roman, Julia Santiago |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
malectin-like receptor kinases
0301 basic medicine 0106 biological sciences membrane receptors Glycosylation Catharanthus Protein Conformation Arabidopsis cell-wall signalling plant reproductive signalling Crystallography X-Ray 01 natural sciences 03 medical and health sciences chemistry.chemical_compound receptor kinases Protein Domains Structural Biology Cell surface receptor Protein Interaction Domains and Motifs Binding site Receptor Plant Proteins 030304 developmental biology Arabidopsis Proteins/chemistry Binding Sites Calcium/pharmacology Catharanthus/enzymology Plant Proteins/chemistry Protein Kinases/chemistry Protein Kinases/physiology Reproduction Catharanthus roseus cell signalling membrane signalling 0303 health sciences biology Arabidopsis Proteins Chemistry Kinase food and beverages biology.organism_classification Ligand (biochemistry) Research Papers Cell biology 030104 developmental biology Calcium Protein Kinases Linker 010606 plant biology & botany |
| Zdroj: | Acta crystallographica. Section D, Structural biology, vol. 74, no. Pt 7, pp. 671-680 Acta Crystallographica. Section D, Structural Biology bioRxiv |
| Popis: | The biochemical and crystallographic characterization of different Catharanthus roseus receptor kinase 1-like membrane receptors is reported as a first step to understand cell-wall sensing and signalling mechanisms in plants. 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. |
| Databáze: | OpenAIRE |
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