PDBsum entry 6fig

Plant protein

PDB id: 6fig

Contents

Protein chains

386 a.a.

Ligands

NAG-NAG ×4

NAG-NAG-FUC

EDO

NAG

CIT

Metals

_CA ×4

Waters ×743

PDB id:

6fig

Name:

Plant protein

Title:

Crystal structure of the anx1 ectodomain from arabidopsis thaliana

Structure:

Receptor-like protein kinase anxur1. Chain: a, b. Engineered: yes

Source:

Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: anx1, at3g04690, f7o18.16. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: tnao38.

Resolution:

1.48Å R-factor: 0.172 R-free: 0.192

Authors:

J.Santiago

Key ref:

S.Moussu et al. (2018). Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction. Acta Crystallogr D Struct Biol, 74, 671-680. PubMed id: 29968676

Date:

18-Jan-18 Release date: 11-Jul-18

Protein chains

Q9SR05  (ANX1_ARATH) -  Receptor-like protein kinase ANXUR1 from Arabidopsis thaliana

Seq: 850 a.a.

Struc: 386 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] (Bound ligand (Het Group name = NAG) matches with 41.38% similarity) + ADP + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Acta Crystallogr D Struct Biol 74:671-680 (2018)

PubMed id: 29968676

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

S.Moussu, S.Augustin, A.O.Roman, C.Broyart, J.Santiago.

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.