5y9w | pdb_00005y9w
Crystal 1 for AtLURE1.2-AtPRK6LRR
Structural highlights
FunctionPRK6_ARATH Key receptor for sensing species-specific attractants in cooperation with other pollen receptor-like kinases. Essential for pollen tube reorientation toward attractant peptides.[1] Publication Abstract from PubMedTransportation 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(LRR)) 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. Structural basis for receptor recognition of pollen tube attraction peptides.,Zhang X, Liu W, Nagae TT, Takeuchi H, Zhang H, Han Z, Higashiyama T, Chai J Nat Commun. 2017 Nov 6;8(1):1331. doi: 10.1038/s41467-017-01323-8. PMID:29109411[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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