7xvg

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'''Unreleased structure'''
 
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The entry 7xvg is ON HOLD until Paper Publication
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==Cryo-EM structure of binary complex of plant NLR Sr35 and effector AvrSr35==
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<StructureSection load='7xvg' size='340' side='right'caption='[[7xvg]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7xvg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Puccinia_graminis_f._sp._tritici Puccinia graminis f. sp. tritici] and [https://en.wikipedia.org/wiki/Triticum_monococcum Triticum monococcum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XVG FirstGlance]. <br>
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</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=7xvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xvg OCA], [https://pdbe.org/7xvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xvg RCSB], [https://www.ebi.ac.uk/pdbsum/7xvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xvg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/A0A5B0N367_PUCGR A0A5B0N367_PUCGR]]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Nucleotide-binding, leucine-rich repeat receptors (NLRs) perceive pathogen effectors to trigger plant immunity. The direct recognition mechanism of pathogen effectors by coiled-coil NLRs (CNLs) remains unclear. We demonstrate that the Triticum monococcum CNL Sr35 directly recognizes the pathogen effector AvrSr35 from Puccinia graminis f. sp. tritici and report a cryo-electron microscopy structure of Sr35 resistosome and a crystal structure of AvrSr35. We show that AvrSr35 forms homodimers that are disassociated into monomers upon direct recognition by the leucine-rich repeat domain of Sr35, which induces Sr35 resistosome assembly and the subsequent immune response. The first 20 amino-terminal residues of Sr35 are indispensable for immune signaling but not for plasma membrane association. Our findings reveal the direct recognition and activation mechanism of a plant CNL and provide insights into biochemical function of Sr35 resistosome.
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Authors:
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Pathogen effector AvrSr35 triggers Sr35 resistosome assembly via a direct recognition mechanism.,Zhao YB, Liu MX, Chen TT, Ma X, Li ZK, Zheng Z, Zheng SR, Chen L, Li YZ, Tang LR, Chen Q, Wang P, Ouyang S Sci Adv. 2022 Sep 9;8(36):eabq5108. doi: 10.1126/sciadv.abq5108. Epub 2022 Sep 9. PMID:36083908<ref>PMID:36083908</ref>
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Description:
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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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<div class="pdbe-citations 7xvg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Puccinia graminis f. sp. tritici]]
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[[Category: Triticum monococcum]]
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[[Category: Li ZK]]
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[[Category: Liu MX]]
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[[Category: Ouyang SY]]
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[[Category: Zhao YB]]

Revision as of 06:20, 28 September 2022

Cryo-EM structure of binary complex of plant NLR Sr35 and effector AvrSr35

PDB ID 7xvg

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