5YAH

Crystal 2 for AtLURE1.2-AtPRK6LRR

5YAH の概要

• エントリーDOI: 10.2210/pdb5yah/pdb
• 分子名称: Pollen receptor-like kinase 6, Protein LURE 1.2 (3 entities in total)
• 機能のキーワード: cysteine-rich peptides, leucine-rich repeat receptor kinase, receptor-ligand complex, pollen tube guidance, plant protein, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : Q3E991; Secreted : Q4VP08
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35143.89

構造登録者

Chai, J.,Zhang, X. (登録日: 2017-08-31, 公開日: 2018-04-11)

主引用文献

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

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: 29109411
DOI: 10.1038/s41467-017-01323-8

実験手法

X-RAY DIFFRACTION (2.104 Å)