5gr8

From Proteopedia

(Difference between revisions)

Revision as of 19:05, 15 December 2016

Crystal structure of PEPR1-AtPEP1

Structural highlights

5gr8 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
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).^[1] ^[2] [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.^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yamaguchi Y, Pearce G, Ryan CA. The cell surface leucine-rich repeat receptor for AtPep1, an endogenous peptide elicitor in Arabidopsis, is functional in transgenic tobacco cells. Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10104-9. Epub 2006 Jun 19. PMID:16785433 doi:http://dx.doi.org/10.1073/pnas.0603729103
↑ Liu Z, Wu Y, Yang F, Zhang Y, Chen S, Xie Q, Tian X, Zhou JM. BIK1 interacts with PEPRs to mediate ethylene-induced immunity. Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):6205-10. doi:, 10.1073/pnas.1215543110. Epub 2013 Feb 19. PMID:23431184 doi:http://dx.doi.org/10.1073/pnas.1215543110
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5gr8"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5gr8 is ON HOLD
+==Crystal structure of PEPR1-AtPEP1==
+<StructureSection load='5gr8' size='340' side='right' caption='[[5gr8]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
+== 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>
+</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>
+<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='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>
+</table>
+== 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>
+<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.
-Authors: Chai, J.J., Tang, J.
+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>
-Description: Crystal structure of PEPR1-AtPEP1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5gr8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Non-specific serine/threonine protein kinase]]
+[[Category: Chai, J J]]
 [[Category: Tang, J]]
-[[Category: Chai, J.J]]
+[[Category: Atpep1]]
+[[Category: Damp]]
+[[Category: Pepr1]]
+[[Category: Prr]]
+[[Category: Transferase]]

5gr8

From Proteopedia

Revision as of 19:05, 15 December 2016

Crystal structure of PEPR1-AtPEP1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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