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| ==Crystal structure of the BIR3 - SERK2 complex from Arabidopsis thaliana.== | | ==Crystal structure of the BIR3 - SERK2 complex from Arabidopsis thaliana.== |
- | <StructureSection load='6g3w' size='340' side='right' caption='[[6g3w]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='6g3w' size='340' side='right'caption='[[6g3w]], [[Resolution|resolution]] 2.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6g3w]] is a 4 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=6G3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G3W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6g3w]] 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=6G3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G3W FirstGlance]. <br> |
- | </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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.2Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fg8|6fg8]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SERK2, At1g34210, F23M19.11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), At1g27190, T7N9.25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=6g3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g3w OCA], [https://pdbe.org/6g3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g3w RCSB], [https://www.ebi.ac.uk/pdbsum/6g3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g3w ProSAT]</span></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=6g3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g3w OCA], [http://pdbe.org/6g3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g3w RCSB], [http://www.ebi.ac.uk/pdbsum/6g3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g3w ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
- | == Function == | |
- | [[http://www.uniprot.org/uniprot/SERK2_ARATH SERK2_ARATH]] Serine/threonine-kinase involved in brassinosteroid-dependent and -independent signaling pathways. Acts redundantly with SERK1 as a control point for sporophytic development controlling male gametophyte production.<ref>PMID:18667726</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: Non-specific serine/threonine protein kinase]] | + | [[Category: Large Structures]] |
- | [[Category: Hohmann, U]] | + | [[Category: Hohmann U]] |
- | [[Category: Hothorn, M]] | + | [[Category: Hothorn M]] |
- | [[Category: Ectodomain]]
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- | [[Category: Leucine rich repeat receptor]]
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- | [[Category: Membrane receptor]]
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- | [[Category: Negative regulator]]
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- | [[Category: Protein binding]]
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- | [[Category: Pseudokinase]]
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- | [[Category: Receptor complex]]
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| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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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