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| | <StructureSection load='2xcm' size='340' side='right'caption='[[2xcm]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2xcm' size='340' side='right'caption='[[2xcm]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xcm]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath] and [http://en.wikipedia.org/wiki/Barley Barley]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XCM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XCM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xcm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XCM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jki|2jki]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2xcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xcm OCA], [http://pdbe.org/2xcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xcm RCSB], [http://www.ebi.ac.uk/pdbsum/2xcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xcm 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=2xcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xcm OCA], [https://pdbe.org/2xcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xcm RCSB], [https://www.ebi.ac.uk/pdbsum/2xcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xcm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RAR1_ARATH RAR1_ARATH]] Required specifically for plant innate immunity. Is essential for resistance conferred by multiple R genes recognizing different bacterial and oomycete pathogen isolates like avirulent P.syringae or H.parasitica (downy mildew). Contributes additively with SGT1B to RPP5-dependent resistance. Functions as positive regulator of RPS5 accumulation by assisting its stabilization. May function as co-chaperone of HSP90-2 to positively regulate the steady-state accumulation of RPM1 and protect it from SGT1-mediated degradation. Acts as negative regulator of pathogen-associated molecular pattern (PAMP)-triggered immunity.<ref>PMID:11847308</ref> <ref>PMID:12034891</ref> <ref>PMID:12034893</ref> <ref>PMID:14592967</ref> <ref>PMID:15976272</ref> <ref>PMID:17148606</ref> <ref>PMID:19304739</ref> <ref>PMID:19487680</ref> [[http://www.uniprot.org/uniprot/SGT1A_ARATH SGT1A_ARATH]] Functions in R gene-mediated resistance, but participates in a lower extent than SGT1B to RPP5-mediated resistance. Not required for RPM1, RPS2, RPS4 and RPS5-mediated resistance. Probably required for SCF-mediated ubiquitination, by coupling HSP90 to SCF complex for ubiquitination of HSP90 client proteins.<ref>PMID:16619029</ref> | + | [https://www.uniprot.org/uniprot/Q7XJ80_HORVU Q7XJ80_HORVU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Barley]] | + | [[Category: Hordeum vulgare]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pearl, L H]] | + | [[Category: Pearl LH]] |
| - | [[Category: Zhang, M]] | + | [[Category: Zhang M]] |
| - | [[Category: Chaperone-protein binding complex]]
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| - | [[Category: Stress response]]
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| Structural highlights
Function
Q7XJ80_HORVU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Hsp90-mediated function of NLR receptors in plant and animal innate immunity depends on the cochaperone Sgt1 and, at least in plants, on a cysteine- and histidine-rich domains (CHORD)-containing protein Rar1. Functionally, CHORD domains are associated with CS domains, either within the same protein, as in the mammalian melusin and Chp1, or in separate but interacting proteins, as in the plant Rar1 and Sgt1. Both CHORD and CS domains are independently capable of interacting with the molecular chaperone Hsp90 and can coexist in complexes with Hsp90. We have now determined the structure of an Hsp90-CS-CHORD ternary complex, providing a framework for understanding the dynamic nature of Hsp90-Rar1-Sgt1 complexes. Mutational and biochemical analyses define the architecture of the ternary complex that recruits nucleotide-binding leucine-rich repeat receptors (NLRs) by manipulating the structural elements to control the ATPase-dependent conformational cycle of the chaperone.
Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors.,Zhang M, Kadota Y, Prodromou C, Shirasu K, Pearl LH Mol Cell. 2010 Jul 30;39(2):269-81. PMID:20670895[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang M, Kadota Y, Prodromou C, Shirasu K, Pearl LH. Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors. Mol Cell. 2010 Jul 30;39(2):269-81. PMID:20670895 doi:10.1016/j.molcel.2010.05.010
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