PDBsum entry 4z5w

Hormone

PDB id: 4z5w

Contents

Protein chains

596 a.a.

Ligands

TYS-ILE-TYS-THR-GLN ×2

NAG-NAG

NAG ×11

Waters ×340

PDB id:

4z5w

Name:

Hormone

Title:

The plant peptide hormone receptor

Structure:

Phytosulfokine receptor 1. Chain: a, b. Fragment: unp residues 24-659. Synonym: dcpskr1,phytosulfokine lrr receptor kinase 1. Engineered: yes. Phytosulfokine. Chain: p, q. Engineered: yes

Source:

Daucus carota. Wild carrot. Organism_taxid: 4039. Gene: pskr. Expressed in: insect cell expression vector ptie1. Expression_system_taxid: 266783. Synthetic: yes. Organism_taxid: 3701

Resolution:

2.20Å R-factor: 0.214 R-free: 0.263

Authors:

J.Chai,J.Wang,Z.Han

Key ref:

J.Wang et al. (2015). Allosteric receptor activation by the plant peptide hormone phytosulfokine. Nature, 525, 265-268. PubMed id: 26308901 DOI: 10.1038/nature14858

Date:

03-Apr-15 Release date: 02-Mar-16

Protein chains

Q8LPB4  (PSKR1_DAUCA) -  Phytosulfokine receptor 1 from Daucus carota

Seq: 1021 a.a.

Struc: 596 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] (Bound ligand (Het Group name = NAG) matches with 41.38% similarity) + ADP + H(+)

L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] (Bound ligand (Het Group name = NAG) matches with 41.38% similarity) + ADP + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1038/nature14858

Nature 525:265-268 (2015)

PubMed id: 26308901

Allosteric receptor activation by the plant peptide hormone phytosulfokine.

J.Wang, H.Li, Z.Han, H.Zhang, T.Wang, G.Lin, J.Chang, W.Yang, J.Chai.

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.