5oes

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'''Unreleased structure'''
 
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The entry 5oes is ON HOLD until Paper Publication
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==The structure of a glutathione synthetase (StGSS1) from Solanum tuberosum in ADP and y-EC bound closed conformation.==
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<StructureSection load='5oes' size='340' side='right'caption='[[5oes]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5oes]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OES FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3GC:GAMMA-GLUTAMYLCYSTEINE'>3GC</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oes OCA], [https://pdbe.org/5oes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oes RCSB], [https://www.ebi.ac.uk/pdbsum/5oes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oes ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/M1CSC4_SOLTU M1CSC4_SOLTU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plant 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.
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Authors: Lilley, C.J., Maqbool, A., Wu, D., Yusup, H.B., Jones, L.M., Birch, P.R.J., Banfield, M.J., Urwin, P.E., Eves-van den Akker, S.
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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<ref>PMID:29641602</ref>
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Description: The structure of a glutathione synthetase (StGSS1) from Solanum tuberosum in ADP and y-EC bound closed conformation.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Urwin, P.E]]
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<div class="pdbe-citations 5oes" style="background-color:#fffaf0;"></div>
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[[Category: Lilley, C.J]]
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[[Category: Yusup, H.B]]
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==See Also==
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[[Category: Maqbool, A]]
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*[[Glutathione synthetase|Glutathione synthetase]]
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[[Category: Eves-Van Den Akker, S]]
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== References ==
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[[Category: Jones, L.M]]
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<references/>
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[[Category: Banfield, M.J]]
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__TOC__
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[[Category: Wu, D]]
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</StructureSection>
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[[Category: Birch, P.R.J]]
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[[Category: Large Structures]]
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[[Category: Solanum tuberosum]]
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[[Category: Banfield MJ]]
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[[Category: Birch PRJ]]
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[[Category: Eves-van den Akker S]]
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[[Category: Jones LM]]
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[[Category: Lilley CJ]]
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[[Category: Maqbool A]]
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[[Category: Urwin PE]]
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[[Category: Wu D]]
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[[Category: Yusup HB]]

Current revision

The structure of a glutathione synthetase (StGSS1) from Solanum tuberosum in ADP and y-EC bound closed conformation.

PDB ID 5oes

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