5oet: Difference between revisions
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<StructureSection load='5oet' size='340' side='right'caption='[[5oet]], [[Resolution|resolution]] 2.57Å' scene=''> | <StructureSection load='5oet' size='340' side='right'caption='[[5oet]], [[Resolution|resolution]] 2.57Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5oet]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OET OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5oet]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Globodera_pallida Globodera pallida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OET FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.57Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oet OCA], [https://pdbe.org/5oet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oet RCSB], [https://www.ebi.ac.uk/pdbsum/5oet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oet ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A183C5H8_GLOPA A0A183C5H8_GLOPA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Globodera pallida]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Banfield MJ]] | ||
[[Category: | [[Category: Birch PRJ]] | ||
[[Category: | [[Category: Eves-van den Akker S]] | ||
[[Category: Jones | [[Category: Jones LM]] | ||
[[Category: Lilley | [[Category: Lilley CJ]] | ||
[[Category: Maqbool | [[Category: Maqbool A]] | ||
[[Category: Urwin | [[Category: Urwin PE]] | ||
[[Category: Wu | [[Category: Wu D]] | ||
[[Category: Yusup | [[Category: Yusup HB]] | ||
Latest revision as of 19:47, 13 December 2023
The structure of a glutathione synthetase like-effector (GSS30) from Globodera pallida in apoform.The structure of a glutathione synthetase like-effector (GSS30) from Globodera pallida in apoform.
Structural highlights
FunctionPublication Abstract from PubMedPlant pathogens and parasites are a major threat to global food security. Plant parasitism has arisen four times independently within the phylum Nematoda, resulting in at least one parasite of every major food crop in the world. Some species within the most economically important order (Tylenchida) secrete proteins termed effectors into their host during infection to re-programme host development and immunity. The precise detail of how nematodes evolve new effectors is not clear. Here we reconstruct the evolutionary history of a novel effector gene family. We show that during the evolution of plant parasitism in the Tylenchida, the housekeeping glutathione synthetase (GS) gene was extensively replicated. New GS paralogues acquired multiple dorsal gland promoter elements, altered spatial expression to the secretory dorsal gland, altered temporal expression to primarily parasitic stages, and gained a signal peptide for secretion. The gene products are delivered into the host plant cell during infection, giving rise to "GS-like effectors". Remarkably, by solving the structure of GS-like effectors we show that during this process they have also diversified in biochemical activity, and likely represent the founding members of a novel class of GS-like enzyme. Our results demonstrate the re-purposing of an endogenous housekeeping gene to form a family of effectors with modified functions. We anticipate that our discovery will be a blueprint to understand the evolution of other plant-parasitic nematode effectors, and the foundation to uncover a novel enzymatic function. Effector gene birth in plant parasitic nematodes: Neofunctionalization of a housekeeping glutathione synthetase gene.,Lilley CJ, Maqbool A, Wu D, Yusup HB, Jones LM, Birch PRJ, Banfield MJ, Urwin PE, Eves-van den Akker S PLoS Genet. 2018 Apr 11;14(4):e1007310. doi: 10.1371/journal.pgen.1007310. PMID:29641602[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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