This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5iyv

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 09:05, 3 October 2016

Crystal structure of the Arabidopsis receptor kinase HAESA LRR ectdomain in complex with the peptide hormone IDL1.

Structural highlights

5iyv is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RLK5_ARATH] Receptor with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates that controls floral organ abscission. May interact with the 'INFLORESCENCE DEFICIENT IN ABSCISSION' (IDA) ligands family.^[1] ^[2] ^[3] [IDL1_ARATH] Involved in an ethylene-independent separation step of floral abscission. May act with RLK5 and HSL2 as ligand-receptor pairs.^[4]

Publication Abstract from PubMed

Plants constantly renew during their life cycle and thus require to shed senescent and damaged organs. Floral abscission is controlled by the leucine-rich repeat receptor kinase (LRR-RK) HAESA and the peptide hormone IDA. It is unknown how expression of IDA in the abscission zone leads to HAESA activation. Here we show that IDA is sensed directly by the HAESA ectodomain. Crystal structures of HAESA in complex with IDA reveal a hormone binding pocket that accommodates an active dodecamer peptide. A central hydroxyproline residue anchors IDA to the receptor. The HAESA co-receptor SERK1, a positive regulator of the floral abscission pathway, allows for high-affinity sensing of the peptide hormone by binding to an Arg-His-Asn motif in IDA. This sequence pattern is conserved among diverse plant peptides, suggesting that plant peptide hormone receptors may share a common ligand binding mode and activation mechanism.

Mechanistic insight into a peptide hormone signaling complex mediating floral organ abscission.,Santiago J, Brandt B, Wildhagen M, Hohmann U, Hothorn LA, Butenko MA, Hothorn M Elife. 2016 Apr 8;5. pii: e15075. doi: 10.7554/eLife.15075. PMID:27058169^[5]

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

References

↑ Jinn TL, Stone JM, Walker JC. HAESA, an Arabidopsis leucine-rich repeat receptor kinase, controls floral organ abscission. Genes Dev. 2000 Jan 1;14(1):108-17. PMID:10640280
↑ Stenvik GE, Tandstad NM, Guo Y, Shi CL, Kristiansen W, Holmgren A, Clark SE, Aalen RB, Butenko MA. The EPIP peptide of INFLORESCENCE DEFICIENT IN ABSCISSION is sufficient to induce abscission in arabidopsis through the receptor-like kinases HAESA and HAESA-LIKE2. Plant Cell. 2008 Jul;20(7):1805-17. doi: 10.1105/tpc.108.059139. Epub 2008 Jul, 25. PMID:18660431 doi:http://dx.doi.org/10.1105/tpc.108.059139
↑ Cho SK, Larue CT, Chevalier D, Wang H, Jinn TL, Zhang S, Walker JC. Regulation of floral organ abscission in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15629-34. doi:, 10.1073/pnas.0805539105. Epub 2008 Sep 22. PMID:18809915 doi:http://dx.doi.org/10.1073/pnas.0805539105
↑ Stenvik GE, Tandstad NM, Guo Y, Shi CL, Kristiansen W, Holmgren A, Clark SE, Aalen RB, Butenko MA. The EPIP peptide of INFLORESCENCE DEFICIENT IN ABSCISSION is sufficient to induce abscission in arabidopsis through the receptor-like kinases HAESA and HAESA-LIKE2. Plant Cell. 2008 Jul;20(7):1805-17. doi: 10.1105/tpc.108.059139. Epub 2008 Jul, 25. PMID:18660431 doi:http://dx.doi.org/10.1105/tpc.108.059139
↑ Santiago J, Brandt B, Wildhagen M, Hohmann U, Hothorn LA, Butenko MA, Hothorn M. Mechanistic insight into a peptide hormone signaling complex mediating floral organ abscission. Elife. 2016 Apr 8;5. pii: e15075. doi: 10.7554/eLife.15075. PMID:27058169 doi:http://dx.doi.org/10.7554/eLife.15075

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/5iyv"

@@ Line 6: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</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=5iyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iyv OCA], [http://pdbe.org/5iyv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iyv RCSB], [http://www.ebi.ac.uk/pdbsum/5iyv PDBsum]</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=5iyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iyv OCA], [http://pdbe.org/5iyv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iyv RCSB], [http://www.ebi.ac.uk/pdbsum/5iyv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iyv ProSAT]</span></td></tr>
 </table>
 == Function ==

5iyv

From Proteopedia

Revision as of 09:05, 3 October 2016

Crystal structure of the Arabidopsis receptor kinase HAESA LRR ectdomain in complex with the peptide hormone IDL1.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox