6xwe

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Current revision (10:43, 23 October 2024) (edit) (undo)
 
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<StructureSection load='6xwe' size='340' side='right'caption='[[6xwe]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
<StructureSection load='6xwe' size='340' side='right'caption='[[6xwe]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6xwe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XWE FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XWE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49&#8491;</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]] 1.49&#8491;</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=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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'>[https://proteopedia.org/fgij/fg.htm?mol=6xwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwe OCA], [https://pdbe.org/6xwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xwe RCSB], [https://www.ebi.ac.uk/pdbsum/6xwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwe 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=6xwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwe OCA], [https://pdbe.org/6xwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xwe RCSB], [https://www.ebi.ac.uk/pdbsum/6xwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwe ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[https://www.uniprot.org/uniprot/LYK3_MEDTR LYK3_MEDTR] Putative receptor for S.meliloti Nod factor signals essential for the establishment of the nitrogen-fixing, root nodule symbiosis with S.meliloti (PubMed:20971894, PubMed:12947035, PubMed:17586690, PubMed:25351493). Involved in the control of root hair curling after S.meliloti infection, probably by modulating the reorganization of the microtubular cytoskeleton in epidermal and cortical cells (PubMed:17586690, PubMed:11290290). Regulates a subset of Nod factor-induced genes (PubMed:17586690).<ref>PMID:11290290</ref> <ref>PMID:12947035</ref> <ref>PMID:17586690</ref> <ref>PMID:20971894</ref> <ref>PMID:25351493</ref>
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Plants evolved lysine motif (LysM) receptors to recognize and parse microbial elicitors and drive intracellular signaling to limit or facilitate microbial colonization. We investigated how chitin and nodulation (Nod) factor receptors of Lotus japonicus initiate differential signaling of immunity or root nodule symbiosis. Two motifs in the LysM1 domains of these receptors determine specific recognition of ligands and discriminate between their in planta functions. These motifs define the ligand-binding site and make up the most structurally divergent regions in cognate Nod factor receptors. An adjacent motif modulates the specificity for Nod factor recognition and determines the selection of compatible rhizobial symbionts in legumes. We also identified how binding specificities in LysM receptors can be altered to facilitate Nod factor recognition and signaling from a chitin receptor, advancing the prospects of engineering rhizobial symbiosis into nonlegumes.
 
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Ligand-recognizing motifs in plant LysM receptors are major determinants of specificity.,Bozsoki Z, Gysel K, Hansen SB, Lironi D, Kronauer C, Feng F, de Jong N, Vinther M, Kamble M, Thygesen MB, Engholm E, Kofoed C, Fort S, Sullivan JT, Ronson CW, Jensen KJ, Blaise M, Oldroyd G, Stougaard J, Andersen KR, Radutoiu S Science. 2020 Aug 7;369(6504):663-670. doi: 10.1126/science.abb3377. PMID:32764065<ref>PMID:32764065</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 6xwe" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Medicago truncatula]]
 
[[Category: Andersen KR]]
[[Category: Andersen KR]]
[[Category: Blaise M]]
[[Category: Blaise M]]
[[Category: Gysel K]]
[[Category: Gysel K]]

Current revision

Crystal structure of LYK3 ectodomain

PDB ID 6xwe

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