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| | <StructureSection load='5w3x' size='340' side='right'caption='[[5w3x]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5w3x' size='340' side='right'caption='[[5w3x]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5w3x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_solanacearum"_smith_1896 "bacillus solanacearum" smith 1896] and [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W3X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5W3X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5w3x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Ralstonia_solanacearum Ralstonia solanacearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W3X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5w40|5w40]], [[5w3y|5w3y]], [[5w3t|5w3t]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">popp, RUN1985_v1_1190012 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=305 "Bacillus solanacearum" Smith 1896]), RRS1, RCH2, RRS1-R, WRKY52 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5w3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w3x OCA], [https://pdbe.org/5w3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w3x RCSB], [https://www.ebi.ac.uk/pdbsum/5w3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w3x ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5w3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w3x OCA], [http://pdbe.org/5w3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w3x RCSB], [http://www.ebi.ac.uk/pdbsum/5w3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w3x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/WR52W_ARATH WR52W_ARATH]] Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Acts also as a disease resistance protein involved in resistance to fungal and bacterial pathogens, including R.solanacearum, P.syringae pv. tomato and C.higginsianum. In presence of RPS4, elicites an EDS1-dependent hypersensitive response (PubMed:24146667).[UniProtKB:Q9FH83]<ref>PMID:19519800</ref> <ref>PMID:19826224</ref> <ref>PMID:24146667</ref> | + | [https://www.uniprot.org/uniprot/A0A0S4VB05_RALSL A0A0S4VB05_RALSL] |
| | <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: Bacillus solanacearum smith 1896]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Arath]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gao, L]] | + | [[Category: Ralstonia solanacearum]] |
| - | [[Category: Song, J]] | + | [[Category: Gao L]] |
| - | [[Category: Zhang, Z M]] | + | [[Category: Song J]] |
| - | [[Category: Ip6]] | + | [[Category: Zhang ZM]] |
| - | [[Category: Popp2]]
| + | |
| - | [[Category: Rrs-r]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Wrky]]
| + | |
| - | [[Category: Yopj effector]]
| + | |
| Structural highlights
Function
A0A0S4VB05_RALSL
Publication Abstract from PubMed
The Yersinia outer protein J (YopJ) family of bacterial effectors depends on a novel acetyltransferase domain to acetylate signalling proteins from plant and animal hosts. However, the underlying mechanism is unclear. Here, we report the crystal structures of PopP2, a YopJ effector produced by the plant pathogen Ralstonia solanacearum, in complex with inositol hexaphosphate (InsP6), acetyl-coenzyme A (AcCoA) and/or substrate Resistance to Ralstonia solanacearum 1 (RRS1-R)WRKY. PopP2 recognizes the WRKYGQK motif of RRS1-RWRKY to position a targeted lysine in the active site for acetylation. Importantly, the PopP2-RRS1-RWRKY association is allosterically regulated by InsP6 binding, suggesting a previously unidentified role of the eukaryote-specific cofactor in substrate interaction. Furthermore, we provide evidence for the reaction intermediate of PopP2-mediated acetylation, an acetyl-cysteine covalent adduct, lending direct support to the 'ping-pong'-like catalytic mechanism proposed for YopJ effectors. Our study provides critical mechanistic insights into the virulence activity of YopJ class of acetyltransferases.
Mechanism of host substrate acetylation by a YopJ family effector.,Zhang ZM, Ma KW, Gao L, Hu Z, Schwizer S, Ma W, Song J Nat Plants. 2017 Jul 24;3:17115. doi: 10.1038/nplants.2017.115. PMID:28737762[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang ZM, Ma KW, Gao L, Hu Z, Schwizer S, Ma W, Song J. Mechanism of host substrate acetylation by a YopJ family effector. Nat Plants. 2017 Jul 24;3:17115. doi: 10.1038/nplants.2017.115. PMID:28737762 doi:http://dx.doi.org/10.1038/nplants.2017.115
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