View source for 5nnw


==NLPPya in complex with glucosamine==
<StructureSection load='5nnw' size='340' side='right'caption='[[5nnw]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nnw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pythium_aphanidermatum Pythium aphanidermatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NNW 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]] 1.54&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCS:D-GLUCOSAMINE'>GCS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5nnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nnw OCA], [https://pdbe.org/5nnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nnw RCSB], [https://www.ebi.ac.uk/pdbsum/5nnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nnw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9SPD4_PYTAP Q9SPD4_PYTAP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Necrosis and ethylene-inducing peptide 1-like (NLP) proteins constitute a superfamily of proteins produced by plant pathogenic bacteria, fungi, and oomycetes. Many NLPs are cytotoxins that facilitate microbial infection of eudicot, but not of monocot plants. Here, we report glycosylinositol phosphorylceramide (GIPC) sphingolipids as NLP toxin receptors. Plant mutants with altered GIPC composition were more resistant to NLP toxins. Binding studies and x-ray crystallography showed that NLPs form complexes with terminal monomeric hexose moieties of GIPCs that result in conformational changes within the toxin. Insensitivity to NLP cytolysins of monocot plants may be explained by the length of the GIPC head group and the architecture of the NLP sugar-binding site. We unveil early steps in NLP cytolysin action that determine plant clade-specific toxin selectivity.

Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins.,Lenarcic T, Albert I, Bohm H, Hodnik V, Pirc K, Zavec AB, Podobnik M, Pahovnik D, Zagar E, Pruitt R, Greimel P, Yamaji-Hasegawa A, Kobayashi T, Zienkiewicz A, Gomann J, Mortimer JC, Fang L, Mamode-Cassim A, Deleu M, Lins L, Oecking C, Feussner I, Mongrand S, Anderluh G, Nurnberger T Science. 2017 Dec 15;358(6369):1431-1434. doi: 10.1126/science.aan6874. PMID:29242345<ref>PMID:29242345</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nnw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pythium aphanidermatum]]
[[Category: Anderluh G]]
[[Category: Lenarcic T]]
[[Category: Podobnik M]]