4Z5W

The plant peptide hormone receptor

Summary for 4Z5W

• Entry DOI: 10.2210/pdb4z5w/pdb
• Related: 4Z61 4Z62 4Z63 4Z64
• Descriptor: Phytosulfokine receptor 1, Phytosulfokine, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: receptor, hormone
• Biological source: Daucus carota (Wild carrot); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: Q8LPB4
• Total number of polymer chains: 4
• Total formula weight: 144831.45

Authors

Chai, J.,Wang, J.,Han, Z. (deposition date: 2015-04-03, release date: 2016-03-02, Last modification date: 2024-11-20)

Primary citation

Wang, J.,Li, H.,Han, Z.,Zhang, H.,Wang, T.,Lin, G.,Chang, J.,Yang, W.,Chai, J.
Allosteric receptor activation by the plant peptide hormone phytosulfokine
Nature, 525:265-268, 2015

PubMed Abstract: Phytosulfokine (PSK) is a disulfated pentapeptide that has a ubiquitous role in plant growth and development. PSK is perceived by its receptor PSKR, a leucine-rich repeat receptor kinase (LRR-RK). The mechanisms underlying the recognition of PSK, the activation of PSKR and the identity of the components downstream of the initial binding remain elusive. Here we report the crystal structures of the extracellular LRR domain of PSKR in free, PSK- and co-receptor-bound forms. The structures reveal that PSK interacts mainly with a β-strand from the island domain of PSKR, forming an anti-β-sheet. The two sulfate moieties of PSK interact directly with PSKR, sensitizing PSKR recognition of PSK. Supported by biochemical, structural and genetic evidence, PSK binding enhances PSKR heterodimerization with the somatic embryogenesis receptor-like kinases (SERKs). However, PSK is not directly involved in PSKR-SERK interaction but stabilizes PSKR island domain for recruitment of a SERK. Our data reveal the structural basis for PSKR recognition of PSK and allosteric activation of PSKR by PSK, opening up new avenues for the design of PSKR-specific small molecules.

PubMed: 26308901
DOI: 10.1038/nature14858

Experimental method

X-RAY DIFFRACTION (2.2 Å)