View source for 6qbe


==Crystal structure of non-toxic HaNLP3 protein==
<StructureSection load='6qbe' size='340' side='right'caption='[[6qbe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qbe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyaloperonospora_arabidopsidis Hyaloperonospora arabidopsidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QBE 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&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6qbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qbe OCA], [https://pdbe.org/6qbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qbe RCSB], [https://www.ebi.ac.uk/pdbsum/6qbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qbe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H6W1B5_HYAAB H6W1B5_HYAAB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins (NLPs) are secreted by several phytopathogenic microorganisms. They trigger necrosis in various eudicot plants upon binding to plant sphingolipid glycosylinositol phosphorylceramides (GIPC). Interestingly, HaNLP3 from the obligate biotroph oomycete Hyaloperonospora arabidopsidis does not induce necrosis. We determined the crystal structure of HaNLP3 and showed that it adopts the NLP fold. However, the conformations of the loops surrounding the GIPC headgroup-binding cavity differ from those of cytotoxic Pythium aphanidermatum NLPPya. Essential dynamics extracted from mus-long molecular dynamics (MD) simulations reveals a limited conformational plasticity of the GIPC-binding cavity in HaNLP3 relative to toxic NLPs. This likely precludes HaNLP3 binding to GIPCs, which is the underlying reason for the lack of toxicity. This study reveals that mutations at key protein regions cause a switch between non-toxic and toxic phenotypes within the same protein scaffold. Altogether, these data provide evidence that protein flexibility is a distinguishing trait of toxic NLPs and highlight structural determinants for a potential functional diversification of non-toxic NLPs utilized by biotrophic plant pathogens.

Molecular basis for functional diversity among microbial Nep1-like proteins.,Lenarcic T, Pirc K, Hodnik V, Albert I, Borisek J, Magistrato A, Nurnberger T, Podobnik M, Anderluh G PLoS Pathog. 2019 Sep 3;15(9):e1007951. doi: 10.1371/journal.ppat.1007951. , eCollection 2019 Sep. PMID:31479498<ref>PMID:31479498</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qbe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hyaloperonospora arabidopsidis]]
[[Category: Large Structures]]
[[Category: Anderluh G]]
[[Category: Lenarcic T]]
[[Category: Podobnik M]]