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PDBsum entry 6fig
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Plant protein
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PDB id
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6fig
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References listed in PDB file
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Key reference
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Title
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Crystal structures of two tandem malectin-Like receptor kinases involved in plant reproduction.
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Authors
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S.Moussu,
S.Augustin,
A.O.Roman,
C.Broyart,
J.Santiago.
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Ref.
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Acta Crystallogr D Struct Biol, 2018,
74,
671-680.
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PubMed id
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Abstract
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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.
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