2lai
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lai]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyaloperonospora_parasitica Hyaloperonospora parasitica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LAI FirstGlance]. <br> | <table><tr><td colspan='2'>[[2lai]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyaloperonospora_parasitica Hyaloperonospora parasitica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LAI FirstGlance]. <br> | ||
| - | </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=2lai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lai OCA], [https://pdbe.org/2lai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lai RCSB], [https://www.ebi.ac.uk/pdbsum/2lai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lai ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lai OCA], [https://pdbe.org/2lai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lai RCSB], [https://www.ebi.ac.uk/pdbsum/2lai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lai ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ATR13_HYAAB ATR13_HYAAB] Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein RPP13. Recognition of ATR13 by RPP13 initiates defense responses that are effective against oomycete, bacterial and viral pathogens (PubMed:15591208, PubMed:18165328, PubMed:18198274, PubMed:22194907). The allele ATR13-Emco5 recognizes RPP13-Nd, the RPP13 defense protein from Arabidopsis thaliana ecotype Niederzenz (PubMed:19523099).<ref>PMID:15591208</ref> <ref>PMID:18165328</ref> <ref>PMID:18198274</ref> <ref>PMID:19523099</ref> <ref>PMID:22194907</ref> | [https://www.uniprot.org/uniprot/ATR13_HYAAB ATR13_HYAAB] Secreted effector that acts as an elicitor of hypersensitive response (HR) specifically on plants carrying defense protein RPP13. Recognition of ATR13 by RPP13 initiates defense responses that are effective against oomycete, bacterial and viral pathogens (PubMed:15591208, PubMed:18165328, PubMed:18198274, PubMed:22194907). The allele ATR13-Emco5 recognizes RPP13-Nd, the RPP13 defense protein from Arabidopsis thaliana ecotype Niederzenz (PubMed:19523099).<ref>PMID:15591208</ref> <ref>PMID:18165328</ref> <ref>PMID:18198274</ref> <ref>PMID:19523099</ref> <ref>PMID:22194907</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The oomycete Hyaloperonospora arabidopsidis (Hpa) is the causal agent of downy mildew on the model plant Arabidopsis thaliana and has been adapted as a model system to investigate pathogen virulence strategies and plant disease resistance mechanisms. Recognition of Hpa infection occurs when plant resistance proteins (R-genes) detect the presence or activity of pathogen-derived protein effectors delivered to the plant host. This study examines the Hpa effector ATR13 Emco5 and its recognition by RPP13-Nd, the cognate R-gene that triggers programmed cell death (HR) in the presence of recognized ATR13 variants. Herein, we use NMR to solve the backbone structure of ATR13 Emco5, revealing both a helical domain and a disordered internal loop. Additionally, we use site-directed and random mutagenesis to identify several amino acid residues involved in the recognition response conferred by RPP13-Nd. Using our structure as a scaffold, we map these residues to one of two surface-exposed patches of residues under diversifying selection. Exploring possible roles of the disordered region within the ATR13 structure, we perform domain swapping experiments and identify a peptide sequence involved in nucleolar localization. We conclude that ATR13 is a highly dynamic protein with no clear structural homologues that contains two surface-exposed patches of polymorphism, only one of which is involved in RPP13-Nd recognition specificity. | ||
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| - | Structural Elucidation and Functional Characterization of the Hyaloperonospora arabidopsidis Effector Protein ATR13.,Leonelli L, Pelton J, Schoeffler A, Dahlbeck D, Berger J, Wemmer DE, Staskawicz B PLoS Pathog. 2011 Dec;7(12):e1002428. Epub 2011 Dec 15. PMID:22194684<ref>PMID:22194684</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2lai" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Hyaloperonospora arabidopsidis Effector Protein ATR13
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