5gr8 | pdb_00005gr8

Crystal structure of PEPR1-AtPEP1

spinqualitylabelsall models 5gr8, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gr8 is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.587Å Ligands: NAG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PEPR1_ARATH Acts as a receptor for PEP defense peptides. Unlike typical immune receptors, senses an endogenous elicitor that potentiates pathogen-associated molecular pattern (PAMP)-inducible plant responses. Involved in PAMP-triggered immunity (PTI) signaling. Interacts with and phosphorylates the kinase BIK1, a central rate-limiting kinase in PTI signaling (PubMed:23431184). Publication Abstract from PubMed The endogenous peptides AtPep1-8 in Arabidopsis mature from the conserved C-terminal portions of their precursor proteins PROPEP1-8, respectively. The two homologous leucine-rich repeat-receptor kinases (LRR-RKs) PEPR1 and PEPR2 act as receptors of AtPeps. AtPep binding leads to stable association of PEPR1,2 with the shared receptor LRR-RK BAK1, eliciting immune responses similar to those induced by pathogens. Here we report a crystal structure of the extracellular LRR domain of PEPR1 (PEPR1LRR) in complex with AtPep1. The structure reveals that AtPep1 adopts a fully extended conformation and binds to the inner surface of the superhelical PEPR1LRR. Biochemical assays showed that AtPep1 is capable of inducing PEPR1LRR-BAK1LRR heterodimerization. The conserved C-terminal portion of AtPep1 dominates AtPep1 binding to PEPR1LRR, with the last amino acid of AtPep1 Asn23 forming extensive interactions with PEPR1LRR. Deletion of the last residue of AtPep1 significantly compromised AtPep1 interaction with PEPR1LRR. Together, our data reveal a conserved structural mechanism of AtPep1 recognition by PEPR1, providing significant insight into prediction of recognition of other peptides by their cognate LRR-RKs. Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1.,Tang J, Han Z, Sun Y, Zhang H, Gong X, Chai J Cell Res. 2015 Jan;25(1):110-20. doi: 10.1038/cr.2014.161. Epub 2014 Dec 5. PMID:25475059 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA