5gr8
From Proteopedia
(Difference between revisions)
m (Protected "5gr8" [edit=sysop:move=sysop]) |
|||
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of PEPR1-AtPEP1== | |
| + | <StructureSection load='5gr8' size='340' side='right'caption='[[5gr8]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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'>[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> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == 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<ref>PMID:25475059</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5gr8" style="background-color:#fffaf0;"></div> |
| - | [[Category: Chai | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chai JJ]] | ||
| + | [[Category: Tang J]] | ||
Current revision
Crystal structure of PEPR1-AtPEP1
| |||||||||||
