5Y9W
Crystal 1 for AtLURE1.2-AtPRK6LRR
Summary for 5Y9W
Entry DOI | 10.2210/pdb5y9w/pdb |
Descriptor | Pollen receptor-like kinase 6, Protein LURE 1.2, SULFATE ION, ... (4 entities in total) |
Functional Keywords | cysteine-rich peptide, leucine-rich repeat receptor kinase, receptor-ligand complex, pollen tube guidance, plant protein, transferase |
Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
Cellular location | Cell membrane ; Single-pass type I membrane protein : Q3E991 Secreted : Q4VP08 |
Total number of polymer chains | 3 |
Total formula weight | 62766.82 |
Authors | |
Primary citation | Zhang, X.,Liu, W.,Nagae, T.T.,Takeuchi, H.,Zhang, H.,Han, Z.,Higashiyama, T.,Chai, J. Structural basis for receptor recognition of pollen tube attraction peptides. Nat Commun, 8:1331-1331, 2017 Cited by PubMed Abstract: Transportation of the immobile sperms directed by pollen tubes to the ovule-enclosed female gametophytes is important for plant sexual reproduction. The defensin-like (DEFL) cysteine-rich peptides (CRPs) LUREs play an essential role in pollen tube attraction to the ovule, though their receptors still remain controversial. Here we provide several lines of biochemical evidence showing that the extracellular domain of the leucine-rich repeat receptor kinase (LRR-RK) PRK6 from Arabidopsis thaliana directly interacts with AtLURE1 peptides. Structural study reveals that a C-terminal loop of the LRR domain (AtPRK6) is responsible for recognition of AtLURE1.2, mediated by a set of residues largely conserved among PRK6 homologs from Arabidopsis lyrata and Capsella rubella, supported by in vitro mutagenesis and semi-in-vivo pollen tube growth assays. Our study provides evidence showing that PRK6 functions as a receptor of the LURE peptides in A. thaliana and reveals a unique ligand recognition mechanism of LRR-RKs. PubMed: 29109411DOI: 10.1038/s41467-017-01323-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.847 Å) |
Structure validation
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