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| | <StructureSection load='5od4' size='340' side='right'caption='[[5od4]], [[Resolution|resolution]] 1.10Å' scene=''> | | <StructureSection load='5od4' size='340' side='right'caption='[[5od4]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5od4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144134 Cbs 144134]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OD4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5od4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OD4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SIX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5507 CBS 144134])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5od4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5od4 OCA], [http://pdbe.org/5od4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5od4 RCSB], [http://www.ebi.ac.uk/pdbsum/5od4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5od4 ProSAT]</span></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=5od4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5od4 OCA], [https://pdbe.org/5od4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5od4 RCSB], [https://www.ebi.ac.uk/pdbsum/5od4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5od4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0C4DI32_FUSO4 A0A0C4DI32_FUSO4] |
| | <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: Cbs 144134]] | + | [[Category: Fusarium oxysporum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Banfield, M J]] | + | [[Category: Banfield MJ]] |
| - | [[Category: Hughes, R K]] | + | [[Category: Hughes RK]] |
| - | [[Category: Beta-sandwich]]
| + | |
| - | [[Category: Effector]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
A0A0C4DI32_FUSO4
Publication Abstract from PubMed
Plant pathogens employ effector proteins to manipulate their hosts. Fusarium oxysporum f. sp. lycopersici (Fol), the causal agent of tomato wilt disease, produces effector protein Avr2. Besides being a virulence factor, Avr2 triggers immunity in I-2 carrying tomato (Solanum lycopersicum). Fol strains that evade I-2 recognition carry point mutations in Avr2 (e.g. Avr2R45H ), but retain full virulence. Here we investigate the virulence function of Avr2 and determine its crystal structure. Transgenic tomato and Arabidopsis expressing either wild-type DeltaspAvr2 (deleted signal-peptide) or the DeltaspAvr2R45H variant become hypersusceptible to fungal, and even bacterial infections, suggesting that Avr2 targets a conserved defense mechanism. Indeed, Avr2 transgenic plants are attenuated in immunity-related readouts, including flg22-induced growth inhibition, ROS production and callose deposition. The crystal structure of Avr2 reveals that the protein shares intriguing structural similarity to ToxA from the wheat pathogen Pyrenophora tritici-repentis and to TRAF proteins. The I-2 resistance-breaking Avr2V41M , Avr2R45H and Avr2R46P variants cluster on a surface-presented loop. Structure-guided mutagenesis enabled uncoupling of virulence from I-2-mediated recognition. We conclude that I-2-mediated recognition is not based on monitoring Avr2 virulence activity, which includes suppression of immune responses via an evolutionarily conserved effector target, but by recognition of a distinct epitope.
Structure-function analysis of the Fusarium oxysporum Avr2 effector allows uncoupling of its immune-suppressing activity from recognition.,Di X, Cao L, Hughes RK, Tintor N, Banfield MJ, Takken FLW New Phytol. 2017 Aug 31. doi: 10.1111/nph.14733. PMID:28857169[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Di X, Cao L, Hughes RK, Tintor N, Banfield MJ, Takken FLW. Structure-function analysis of the Fusarium oxysporum Avr2 effector allows uncoupling of its immune-suppressing activity from recognition. New Phytol. 2017 Aug 31. doi: 10.1111/nph.14733. PMID:28857169 doi:http://dx.doi.org/10.1111/nph.14733
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