6qup: Difference between revisions
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==Structural signatures in EPR3 define a unique class of plant carbohydrate receptors== | |||
<StructureSection load='6qup' size='340' side='right'caption='[[6qup]], [[Resolution|resolution]] 1.87Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6qup]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Lotus_japonicus Lotus japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QUP 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]] 1.871Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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=6qup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qup OCA], [https://pdbe.org/6qup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qup RCSB], [https://www.ebi.ac.uk/pdbsum/6qup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qup ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D3KU53_LOTJA D3KU53_LOTJA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Receptor-mediated perception of surface-exposed carbohydrates like lipo- and exo-polysaccharides (EPS) is important for non-self recognition and responses to microbial associated molecular patterns in mammals and plants. In legumes, EPS are monitored and can either block or promote symbiosis with rhizobia depending on their molecular composition. To establish a deeper understanding of receptors involved in EPS recognition, we determined the structure of the Lotus japonicus (Lotus) exopolysaccharide receptor 3 (EPR3) ectodomain. EPR3 forms a compact structure built of three putative carbohydrate-binding modules (M1, M2 and LysM3). M1 and M2 have unique betaalphabetabeta and betaalphabeta folds that have not previously been observed in carbohydrate binding proteins, while LysM3 has a canonical betaalphaalphabeta fold. We demonstrate that this configuration is a structural signature for a ubiquitous class of receptors in the plant kingdom. We show that EPR3 is promiscuous, suggesting that plants can monitor complex microbial communities though this class of receptors. | |||
Structural signatures in EPR3 define a unique class of plant carbohydrate receptors.,Wong JEMM, Gysel K, Birkefeldt TG, Vinther M, Muszynski A, Azadi P, Laursen NS, Sullivan JT, Ronson CW, Stougaard J, Andersen KR Nat Commun. 2020 Jul 30;11(1):3797. doi: 10.1038/s41467-020-17568-9. PMID:32732998<ref>PMID:32732998</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6qup" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lama glama]] | |||
[[Category: Large Structures]] | |||
[[Category: Lotus japonicus]] | |||
[[Category: Andersen KR]] | |||
[[Category: Azadi P]] | |||
[[Category: Birkefeldt TG]] | |||
[[Category: Gysel K]] | |||
[[Category: Laursen NS]] | |||
[[Category: Muszynski A]] | |||
[[Category: Ronson CW]] | |||
[[Category: Stougaard J]] | |||
[[Category: Sullivan JT]] | |||
[[Category: Vinther M]] | |||
[[Category: Wong JE]] | |||
Latest revision as of 15:09, 24 January 2024
Structural signatures in EPR3 define a unique class of plant carbohydrate receptorsStructural signatures in EPR3 define a unique class of plant carbohydrate receptors
Structural highlights
FunctionPublication Abstract from PubMedReceptor-mediated perception of surface-exposed carbohydrates like lipo- and exo-polysaccharides (EPS) is important for non-self recognition and responses to microbial associated molecular patterns in mammals and plants. In legumes, EPS are monitored and can either block or promote symbiosis with rhizobia depending on their molecular composition. To establish a deeper understanding of receptors involved in EPS recognition, we determined the structure of the Lotus japonicus (Lotus) exopolysaccharide receptor 3 (EPR3) ectodomain. EPR3 forms a compact structure built of three putative carbohydrate-binding modules (M1, M2 and LysM3). M1 and M2 have unique betaalphabetabeta and betaalphabeta folds that have not previously been observed in carbohydrate binding proteins, while LysM3 has a canonical betaalphaalphabeta fold. We demonstrate that this configuration is a structural signature for a ubiquitous class of receptors in the plant kingdom. We show that EPR3 is promiscuous, suggesting that plants can monitor complex microbial communities though this class of receptors. Structural signatures in EPR3 define a unique class of plant carbohydrate receptors.,Wong JEMM, Gysel K, Birkefeldt TG, Vinther M, Muszynski A, Azadi P, Laursen NS, Sullivan JT, Ronson CW, Stougaard J, Andersen KR Nat Commun. 2020 Jul 30;11(1):3797. doi: 10.1038/s41467-020-17568-9. PMID:32732998[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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