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| | ==Crystal structure of the BIR2 ectodomain from Arabidopsis thaliana.== | | ==Crystal structure of the BIR2 ectodomain from Arabidopsis thaliana.== |
| - | <StructureSection load='6fg7' size='340' side='right' caption='[[6fg7]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='6fg7' size='340' side='right'caption='[[6fg7]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6fg7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FG7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6fg7]] is a 2 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=6FG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FG7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BIR2, At3g28450, MFJ20.14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fg7 OCA], [http://pdbe.org/6fg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fg7 RCSB], [http://www.ebi.ac.uk/pdbsum/6fg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fg7 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=6fg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fg7 OCA], [https://pdbe.org/6fg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fg7 RCSB], [https://www.ebi.ac.uk/pdbsum/6fg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fg7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BIR2_ARATH BIR2_ARATH]] Pseudokinases lacking protein kinase activity and unable to bind ATP-analogs (PubMed:24556575). Negative regulator of pathogen-associated molecular patterns- (PAMP-) triggered immunity by limiting BAK1-receptor complex formation in the absence of ligands (PubMed:24388849).<ref>PMID:24388849</ref> <ref>PMID:24556575</ref> | + | [https://www.uniprot.org/uniprot/BIR2_ARATH BIR2_ARATH] Pseudokinases lacking protein kinase activity and unable to bind ATP-analogs (PubMed:24556575). Negative regulator of pathogen-associated molecular patterns- (PAMP-) triggered immunity by limiting BAK1-receptor complex formation in the absence of ligands (PubMed:24388849).<ref>PMID:24388849</ref> <ref>PMID:24556575</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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Hohmann, U]] | + | [[Category: Large Structures]] |
| - | [[Category: Hothorn, M]] | + | [[Category: Hohmann U]] |
| - | [[Category: Ectodomain]] | + | [[Category: Hothorn M]] |
| - | [[Category: Leucine rich repeat receptor]]
| + | |
| - | [[Category: Membrane receptor]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Pseudokinase]]
| + | |
| Structural highlights
Function
BIR2_ARATH Pseudokinases lacking protein kinase activity and unable to bind ATP-analogs (PubMed:24556575). Negative regulator of pathogen-associated molecular patterns- (PAMP-) triggered immunity by limiting BAK1-receptor complex formation in the absence of ligands (PubMed:24388849).[1] [2]
Publication Abstract from PubMed
The leucine-rich repeat receptor kinase (LRR-RK) BRASSINOSTEROID INSENSITIVE 1 (BRI1) requires a shape-complementary SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK) co-receptor for brassinosteroid sensing and receptor activation (1) . Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signalling responses (2) . The SERK3 elongated (elg) allele(3-5) maps to the complex interface and shows enhanced brassinosteroid signalling, but surprisingly no tighter binding to the BRI1 ectodomain in vitro. Here, we report that rather than promoting the interaction with BRI1, the elg mutation disrupts the ability of the co-receptor to interact with the ectodomains of BRI1-ASSOCIATED-KINASE1 INTERACTING KINASE (BIR) receptor pseudokinases, negative regulators of LRR-RK signalling (6) . A conserved lateral surface patch in BIR LRR domains is required for targeting SERK co-receptors and the elg allele maps to the core of the complex interface in a 1.25 A BIR3-SERK1 structure. Collectively, our structural, quantitative biochemical and genetic analyses suggest that brassinosteroid signalling complex formation is negatively regulated by BIR receptor ectodomains.
The SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signalling.,Hohmann U, Nicolet J, Moretti A, Hothorn LA, Hothorn M Nat Plants. 2018 May 7. pii: 10.1038/s41477-018-0150-9. doi:, 10.1038/s41477-018-0150-9. PMID:29735985[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Halter T, Imkampe J, Mazzotta S, Wierzba M, Postel S, Bucherl C, Kiefer C, Stahl M, Chinchilla D, Wang X, Nurnberger T, Zipfel C, Clouse S, Borst JW, Boeren S, de Vries SC, Tax F, Kemmerling B. The leucine-rich repeat receptor kinase BIR2 is a negative regulator of BAK1 in plant immunity. Curr Biol. 2014 Jan 20;24(2):134-43. doi: 10.1016/j.cub.2013.11.047. Epub 2014, Jan 2. PMID:24388849 doi:http://dx.doi.org/10.1016/j.cub.2013.11.047
- ↑ Blaum BS, Mazzotta S, Noldeke ER, Halter T, Madlung J, Kemmerling B, Stehle T. Structure of the pseudokinase domain of BIR2, a regulator of BAK1-mediated immune signaling in Arabidopsis. J Struct Biol. 2014 Apr;186(1):112-21. doi: 10.1016/j.jsb.2014.02.005. Epub 2014 , Feb 17. PMID:24556575 doi:http://dx.doi.org/10.1016/j.jsb.2014.02.005
- ↑ Hohmann U, Nicolet J, Moretti A, Hothorn LA, Hothorn M. The SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signalling. Nat Plants. 2018 May 7. pii: 10.1038/s41477-018-0150-9. doi:, 10.1038/s41477-018-0150-9. PMID:29735985 doi:http://dx.doi.org/10.1038/s41477-018-0150-9
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