View source for 7au7


==Crystal structure of Nod Factor Perception ectodomain==
<StructureSection load='7au7' size='340' side='right'caption='[[7au7]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7au7]] 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=7AU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AU7 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]] 2.547&#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=MAN:ALPHA-D-MANNOSE'>MAN</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=7au7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7au7 OCA], [https://pdbe.org/7au7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7au7 RCSB], [https://www.ebi.ac.uk/pdbsum/7au7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7au7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NFP_MEDTR NFP_MEDTR] During nodulation, plays a central role in nodule organogenesis (PubMed:22874912). Involved in the perception of Nod factors, the first step of recognition of rhizobia prior to nodulation (PubMed:12753588). Necessary in epidermal cells to induce cortical cell divisions leading to nodule primordia formation (PubMed:22874912). Required during root nodule symbiosis with Sinorhizobium meliloti by triggering infection threads and release of bacteria into the cytoplasm of cells in the infection zone of developing nodules, especially in cells derived from the meristem (PubMed:25351493, PubMed:16844829, PubMed:22087221). Promotes plant fitness (e.g. fruit weight and leaf number) (PubMed:23173081).<ref>PMID:12753588</ref> <ref>PMID:16844829</ref> <ref>PMID:22087221</ref> <ref>PMID:22874912</ref> <ref>PMID:23173081</ref> <ref>PMID:25351493</ref>   Involved in resistance to oomycetes (e.g. Aphanomyces euteiches) and to fungi (e.g. Colletotrichum trifolii).<ref>PMID:23432463</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plants and animals use cell surface receptors to sense and interpret environmental signals. In legume symbiosis with nitrogen-fixing bacteria, the specific recognition of bacterial lipochitooligosaccharide (LCO) signals by single-pass transmembrane receptor kinases determines compatibility. Here, we determine the structural basis for LCO perception from the crystal structures of two lysin motif receptor ectodomains and identify a hydrophobic patch in the binding site essential for LCO recognition and symbiotic function. We show that the receptor monitors the composition of the amphiphilic LCO molecules and uses kinetic proofreading to control receptor activation and signaling specificity. We demonstrate engineering of the LCO binding site to fine-tune ligand selectivity and correct binding kinetics required for activation of symbiotic signaling in plants. Finally, the hydrophobic patch is found to be a conserved structural signature in this class of LCO receptors across legumes that can be used for in silico predictions. Our results provide insights into the mechanism of cell-surface receptor activation by kinetic proofreading of ligands and highlight the potential in receptor engineering to capture benefits in plant-microbe interactions.

Kinetic proofreading of lipochitooligosaccharides determines signal activation of symbiotic plant receptors.,Gysel K, Laursen M, Thygesen MB, Lironi D, Bozsoki Z, Hjuler CT, Maolanon NN, Cheng J, Bjork PK, Vinther M, Madsen LH, Rubsam H, Muszynski A, Ghodrati A, Azadi P, Sullivan JT, Ronson CW, Jensen KJ, Blaise M, Radutoiu S, Stougaard J, Andersen KR Proc Natl Acad Sci U S A. 2021 Nov 2;118(44). pii: 2111031118. doi:, 10.1073/pnas.2111031118. PMID:34716271<ref>PMID:34716271</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7au7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Medicago truncatula]]
[[Category: Andersen KR]]
[[Category: Blaise M]]
[[Category: Gysel K]]