5no9: Difference between revisions
New page: '''Unreleased structure''' The entry 5no9 is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==NLPPya in complex with mannosamine== | |||
<StructureSection load='5no9' size='340' side='right'caption='[[5no9]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5no9]] 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=5NO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NO9 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]] 1.75Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=95Z:(2~{S},3~{S},4~{R},5~{S},6~{R})-3-azanyl-6-(hydroxymethyl)oxane-2,4,5-triol'>95Z</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=5no9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5no9 OCA], [https://pdbe.org/5no9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5no9 RCSB], [https://www.ebi.ac.uk/pdbsum/5no9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5no9 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5no9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pythium aphanidermatum]] | |||
[[Category: Anderluh G]] | |||
[[Category: Lenarcic T]] | |||
[[Category: Podobnik M]] | |||
Latest revision as of 15:03, 6 November 2024
NLPPya in complex with mannosamineNLPPya in complex with mannosamine
Structural highlights
FunctionPublication Abstract from PubMedNecrosis 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||