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| | ==Crystal structure of PEPR1-AtPEP1== | | ==Crystal structure of PEPR1-AtPEP1== |
| - | <StructureSection load='5gr8' size='340' side='right' caption='[[5gr8]], [[Resolution|resolution]] 2.59Å' scene=''> | + | <StructureSection load='5gr8' size='340' side='right'caption='[[5gr8]], [[Resolution|resolution]] 2.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gr8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GR8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gr8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GR8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.587Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gr8 OCA], [http://pdbe.org/5gr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gr8 RCSB], [http://www.ebi.ac.uk/pdbsum/5gr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gr8 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gr8 OCA], [https://pdbe.org/5gr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gr8 RCSB], [https://www.ebi.ac.uk/pdbsum/5gr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gr8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PEPR1_ARATH 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).<ref>PMID:16785433</ref> <ref>PMID:23431184</ref> [[http://www.uniprot.org/uniprot/PEP1_ARATH PEP1_ARATH]] Elicitor of plant defense. Induces the production of plant defensin (PDF1.2) and of H(2)O(2). Promotes resistance to the root fungal pathogen P.irregulare.<ref>PMID:16785434</ref> | + | [https://www.uniprot.org/uniprot/PEP1_ARATH PEP1_ARATH] Elicitor of plant defense. Induces the production of plant defensin (PDF1.2) and of H(2)O(2). Promotes resistance to the root fungal pathogen P.irregulare.<ref>PMID:16785434</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Non-specific serine/threonine protein kinase]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Chai, J J]] | + | [[Category: Large Structures]] |
| - | [[Category: Tang, J]] | + | [[Category: Chai JJ]] |
| - | [[Category: Atpep1]] | + | [[Category: Tang J]] |
| - | [[Category: Damp]]
| + | |
| - | [[Category: Pepr1]]
| + | |
| - | [[Category: Prr]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PEP1_ARATH Elicitor of plant defense. Induces the production of plant defensin (PDF1.2) and of H(2)O(2). Promotes resistance to the root fungal pathogen P.irregulare.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huffaker A, Pearce G, Ryan CA. An endogenous peptide signal in Arabidopsis activates components of the innate immune response. Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10098-103. Epub 2006 Jun 19. PMID:16785434 doi:http://dx.doi.org/0603727103
- ↑ Tang J, Han Z, Sun Y, Zhang H, Gong X, Chai J. Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1. Cell Res. 2015 Jan;25(1):110-20. doi: 10.1038/cr.2014.161. Epub 2014 Dec 5. PMID:25475059 doi:http://dx.doi.org/10.1038/cr.2014.161
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