6a5d

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Current revision (09:18, 22 November 2023) (edit) (undo)
 
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<StructureSection load='6a5d' size='340' side='right'caption='[[6a5d]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='6a5d' size='340' side='right'caption='[[6a5d]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6a5d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A5D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6a5d]] 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=6A5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A5D FirstGlance]. <br>
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</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.401&#8491;</td></tr>
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<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=6a5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a5d OCA], [http://pdbe.org/6a5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a5d RCSB], [http://www.ebi.ac.uk/pdbsum/6a5d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a5d ProSAT]</span></td></tr>
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<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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6a5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a5d OCA], [https://pdbe.org/6a5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a5d RCSB], [https://www.ebi.ac.uk/pdbsum/6a5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a5d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LLG1_ARATH LLG1_ARATH]] Component of the FER-regulated Rho GTPase signaling complex. Acts as a chaperone and coreceptor for FER. Required for localization of FER to the plasma membrane.<ref>PMID:26052747</ref>
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[https://www.uniprot.org/uniprot/LLG1_ARATH LLG1_ARATH] Component of the FER-regulated Rho GTPase signaling complex. Acts as a chaperone and coreceptor for FER. Required for localization of FER to the plasma membrane.<ref>PMID:26052747</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Receptor kinases of the Catharanthus roseus RLK1-like (CrRLK1L) family have emerged as important regulators of plant reproduction, growth and responses to the environment(1). Endogenous RAPID ALKALINIZATION FACTOR (RALF) peptides(2) have previously been proposed as ligands for several members of the CrRLK1L family(1). However, the mechanistic basis of this perception is unknown. Here we report that RALF23 induces a complex between the CrRLK1L FERONIA (FER) and LORELEI (LRE)-LIKE GLYCOSYLPHOSPHATIDYLINOSITOL (GPI)-ANCHORED PROTEIN 1 (LLG1) to regulate immune signalling. Structural and biochemical data indicate that LLG1 (which is genetically important for RALF23 responses) and the related LLG2 directly bind RALF23 to nucleate the assembly of RALF23-LLG1-FER and RALF23-LLG2-FER heterocomplexes, respectively. A conserved N-terminal region of RALF23 is sufficient for the biochemical recognition of RALF23 by LLG1, LLG2 or LLG3, and binding assays suggest that other RALF peptides that share this conserved N-terminal region may be perceived by LLG proteins in a similar manner. Structural data also show that RALF23 recognition is governed by the conformationally flexible C-terminal sides of LLG1, LLG2 and LLG3. Our work reveals a mechanism of peptide perception in plants by GPI-anchored proteins that act together with a phylogenetically unrelated receptor kinase. This provides a molecular framework for understanding how diverse RALF peptides may regulate multiple processes, through perception by distinct heterocomplexes of CrRLK1L receptor kinases and GPI-anchored proteins of the LRE and LLG family.
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Mechanisms of RALF peptide perception by a heterotypic receptor complex.,Xiao Y, Stegmann M, Han Z, DeFalco TA, Parys K, Xu L, Belkhadir Y, Zipfel C, Chai J Nature. 2019 Aug;572(7768):270-274. doi: 10.1038/s41586-019-1409-7. Epub 2019 Jul , 10. PMID:31291642<ref>PMID:31291642</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6a5d" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chai, J]]
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[[Category: Chai J]]
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[[Category: Xiao, Y]]
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[[Category: Xiao Y]]
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[[Category: A plant receptor l1]]
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[[Category: Transferase]]
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Current revision

Crystal structure of plant Glycosylphosphatidylinositol-anchored Protein LLG1

PDB ID 6a5d

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