5zne: Difference between revisions

Revision as of 05:48, 24 October 2018

The crystal structure of immune receptor RGA5A_S of resistance protein Pia from rice (Oryza sativa)

Structural highlights

5zne is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RGA5R_ORYSJ] Disease resistance (R) protein that recognizes the AVR-Pia and AVR1-CO39 effector avirulence proteins from M.oryzae. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Contribution of RGA4 is required to recognize the effector avirulence proteins AVR-Pia and AVR1-CO39 from M.oryzae (PubMed:21251109, PubMed:23548743). Acts as a repressor of the RGA4-mediated cell death activation. Upon infection, recognition and binding of the AVR effectors relieve the RGA5-mediated repression and triggers the hypersensitive response (PubMed:25024433). Immune response triggered by the RGA4-RGA5 -mediated recognition of AVR1-CO39 confers resistance to X.oryzae pathovars (PubMed:27289079).^[1] ^[2] ^[3] ^[4]

References

↑ Okuyama Y, Kanzaki H, Abe A, Yoshida K, Tamiru M, Saitoh H, Fujibe T, Matsumura H, Shenton M, Galam DC, Undan J, Ito A, Sone T, Terauchi R. A multifaceted genomics approach allows the isolation of the rice Pia-blast resistance gene consisting of two adjacent NBS-LRR protein genes. Plant J. 2011 May;66(3):467-79. doi: 10.1111/j.1365-313X.2011.04502.x. Epub 2011 , Mar 7. PMID:21251109 doi:https://dx.doi.org/10.1111/j.1365-313X.2011.04502.x
↑ Cesari S, Thilliez G, Ribot C, Chalvon V, Michel C, Jauneau A, Rivas S, Alaux L, Kanzaki H, Okuyama Y, Morel JB, Fournier E, Tharreau D, Terauchi R, Kroj T. The rice resistance protein pair RGA4/RGA5 recognizes the Magnaporthe oryzae effectors AVR-Pia and AVR1-CO39 by direct binding. Plant Cell. 2013 Apr;25(4):1463-81. doi: 10.1105/tpc.112.107201. Epub 2013 Apr 2. PMID:23548743 doi:https://dx.doi.org/10.1105/tpc.112.107201
↑ Cesari S, Kanzaki H, Fujiwara T, Bernoux M, Chalvon V, Kawano Y, Shimamoto K, Dodds P, Terauchi R, Kroj T. The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance. EMBO J. 2014 Sep 1;33(17):1941-59. doi: 10.15252/embj.201487923. Epub 2014 Jul, 14. PMID:25024433 doi:https://dx.doi.org/10.15252/embj.201487923
↑ Hutin M, Cesari S, Chalvon V, Michel C, Tran TT, Boch J, Koebnik R, Szurek B, Kroj T. Ectopic activation of the rice NLR heteropair RGA4/RGA5 confers resistance to bacterial blight and bacterial leaf streak diseases. Plant J. 2016 Oct;88(1):43-55. doi: 10.1111/tpj.13231. Epub 2016 Aug 18. PMID:27289079 doi:https://dx.doi.org/10.1111/tpj.13231

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OCA

[1] Okuyama Y, Kanzaki H, Abe A, Yoshida K, Tamiru M, Saitoh H, Fujibe T, Matsumura H, Shenton M, Galam DC, Undan J, Ito A, Sone T, Terauchi R. A multifaceted genomics approach allows the isolation of the rice Pia-blast resistance gene consisting of two adjacent NBS-LRR protein genes. Plant J. 2011 May;66(3):467-79. doi: 10.1111/j.1365-313X.2011.04502.x. Epub 2011 , Mar 7. PMID:21251109 doi:https://dx.doi.org/10.1111/j.1365-313X.2011.04502.x

[2] Cesari S, Thilliez G, Ribot C, Chalvon V, Michel C, Jauneau A, Rivas S, Alaux L, Kanzaki H, Okuyama Y, Morel JB, Fournier E, Tharreau D, Terauchi R, Kroj T. The rice resistance protein pair RGA4/RGA5 recognizes the Magnaporthe oryzae effectors AVR-Pia and AVR1-CO39 by direct binding. Plant Cell. 2013 Apr;25(4):1463-81. doi: 10.1105/tpc.112.107201. Epub 2013 Apr 2. PMID:23548743 doi:https://dx.doi.org/10.1105/tpc.112.107201

[3] Cesari S, Kanzaki H, Fujiwara T, Bernoux M, Chalvon V, Kawano Y, Shimamoto K, Dodds P, Terauchi R, Kroj T. The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance. EMBO J. 2014 Sep 1;33(17):1941-59. doi: 10.15252/embj.201487923. Epub 2014 Jul, 14. PMID:25024433 doi:https://dx.doi.org/10.15252/embj.201487923

[4] Hutin M, Cesari S, Chalvon V, Michel C, Tran TT, Boch J, Koebnik R, Szurek B, Kroj T. Ectopic activation of the rice NLR heteropair RGA4/RGA5 confers resistance to bacterial blight and bacterial leaf streak diseases. Plant J. 2016 Oct;88(1):43-55. doi: 10.1111/tpj.13231. Epub 2016 Aug 18. PMID:27289079 doi:https://dx.doi.org/10.1111/tpj.13231

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5zne is ON HOLD  until Paper Publication
+==The crystal structure of immune receptor RGA5A_S of resistance protein Pia from rice (Oryza sativa)==
+<StructureSection load='5zne' size='340' side='right' caption='[[5zne]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5zne]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZNE FirstGlance]. <br>
-Description:
+</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=5zne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zne OCA], [http://pdbe.org/5zne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zne RCSB], [http://www.ebi.ac.uk/pdbsum/5zne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zne ProSAT]</span></td></tr>
-[[Category: Unreleased Structures]]
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RGA5R_ORYSJ RGA5R_ORYSJ]] Disease resistance (R) protein that recognizes the AVR-Pia and AVR1-CO39 effector avirulence proteins from M.oryzae. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Contribution of RGA4 is required to recognize the effector avirulence proteins AVR-Pia and AVR1-CO39 from M.oryzae (PubMed:21251109, PubMed:23548743). Acts as a repressor of the RGA4-mediated cell death activation. Upon infection, recognition and binding of the AVR effectors relieve the RGA5-mediated repression and triggers the hypersensitive response (PubMed:25024433). Immune response triggered by the RGA4-RGA5 -mediated recognition of AVR1-CO39 confers resistance to X.oryzae pathovars (PubMed:27289079).<ref>PMID:21251109</ref> <ref>PMID:23548743</ref> <ref>PMID:25024433</ref> <ref>PMID:27289079</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Guo, L W]]
+[[Category: Huang, D]]
+[[Category: Liu, J F]]
+[[Category: Peng, Y L]]
+[[Category: Plant protein]]
+[[Category: Resistance protein]]
+[[Category: Rga5a_]]
+[[Category: Rice]]

5zne: Difference between revisions

Revision as of 05:48, 24 October 2018

The crystal structure of immune receptor RGA5A_S of resistance protein Pia from rice (Oryza sativa)

Structural highlights

Function

References

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