Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction.

Détails

Ressource 1Télécharger: rr5158.pdf (2924.10 [Ko])
Etat: Serval
Version: Final published version
ID Serval
serval:BIB_465BDE1DAB2A
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction.
Périodique
Acta crystallographica. Section D, Structural biology
Auteur(s)
Moussu S., Augustin S., Roman A.O., Broyart C., Santiago J.
ISSN
2059-7983 (Electronic)
ISSN-L
2059-7983
Statut éditorial
Publié
Date de publication
01/07/2018
Peer-reviewed
Oui
Volume
74
Numéro
Pt 7
Pages
671-680
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
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.
Mots-clé
Arabidopsis Proteins/chemistry, Binding Sites, Calcium/pharmacology, Catharanthus/enzymology, Crystallography, X-Ray, Glycosylation, Plant Proteins/chemistry, Protein Conformation, Protein Domains, Protein Interaction Domains and Motifs, Protein Kinases/chemistry, Protein Kinases/physiology, Reproduction, Arabidopsis, Catharanthus roseus, cell signalling, cell-wall signalling, malectin-like receptor kinases, membrane receptors, membrane signalling, plant reproductive signalling, receptor kinases
Pubmed
Web of science
Open Access
Oui
Création de la notice
17/08/2018 19:56
Dernière modification de la notice
08/05/2019 17:56
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