7mk3

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of NPR1

Structural highlights

7mk3 is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.06Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NPR1_ARATH May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Key positive regulator of the SA-dependent signaling pathway that negatively regulates JA-dependent signaling pathway. Mediates the binding of TGA factors to the as-1 motif found in the pathogenesis-related PR-1 gene, leading to the transcriptional regulation of the gene defense. Controls the onset of systemic acquired resistance (SAR). Upon SAR induction, a biphasic change in cellular reduction potential occurs, resulting in reduction of the cytoplasmic oligomeric form to a monomeric form that accumulates in the nucleus and activates gene expression. Phosphorylated form is target of proteasome degradation.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

NPR1 is a master regulator of the defence transcriptome induced by the plant immune signal salicylic acid(1-4). Despite the important role of NPR1 in plant immunity(5-7), understanding of its regulatory mechanisms has been hindered by a lack of structural information. Here we report cryo-electron microscopy and crystal structures of Arabidopsis NPR1 and its complex with the transcription factor TGA3. Cryo-electron microscopy analysis reveals that NPR1 is a bird-shaped homodimer comprising a central Broad-complex, Tramtrack and Bric-a-brac (BTB) domain, a BTB and carboxyterminal Kelch helix bundle, four ankyrin repeats and a disordered salicylic-acid-binding domain. Crystal structure analysis reveals a unique zinc-finger motif in BTB for interacting with ankyrin repeats and mediating NPR1 oligomerization. We found that, after stimulation, salicylic-acid-induced folding and docking of the salicylic-acid-binding domain onto ankyrin repeats is required for the transcriptional cofactor activity of NPR1, providing a structural explanation for a direct role of salicylic acid in regulating NPR1-dependent gene expression. Moreover, our structure of the TGA32-NPR12-TGA32 complex, DNA-binding assay and genetic data show that dimeric NPR1 activates transcription by bridging two fatty-acid-bound TGA3 dimers to form an enhanceosome. The stepwise assembly of the NPR1-TGA complex suggests possible hetero-oligomeric complex formation with other transcription factors, revealing how NPR1 reprograms the defence transcriptome.

Structural basis of NPR1 in activating plant immunity.,Kumar S, Zavaliev R, Wu Q, Zhou Y, Cheng J, Dillard L, Powers J, Withers J, Zhao J, Guan Z, Borgnia MJ, Bartesaghi A, Dong X, Zhou P Nature. 2022 May;605(7910):561-566. doi: 10.1038/s41586-022-04699-w. Epub 2022, May 11. PMID:35545668^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Delaney TP, Friedrich L, Ryals JA. Arabidopsis signal transduction mutant defective in chemically and biologically induced disease resistance. Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6602-6. doi: 10.1073/pnas.92.14.6602. PMID:11607555 doi:http://dx.doi.org/10.1073/pnas.92.14.6602
↑ Spoel SH, Koornneef A, Claessens SM, Korzelius JP, Van Pelt JA, Mueller MJ, Buchala AJ, Metraux JP, Brown R, Kazan K, Van Loon LC, Dong X, Pieterse CM. NPR1 modulates cross-talk between salicylate- and jasmonate-dependent defense pathways through a novel function in the cytosol. Plant Cell. 2003 Mar;15(3):760-70. doi: 10.1105/tpc.009159. PMID:12615947 doi:http://dx.doi.org/10.1105/tpc.009159
↑ Mou Z, Fan W, Dong X. Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes. Cell. 2003 Jun 27;113(7):935-44. doi: 10.1016/s0092-8674(03)00429-x. PMID:12837250 doi:http://dx.doi.org/10.1016/s0092-8674(03)00429-x
↑ Johnson C, Boden E, Arias J. Salicylic acid and NPR1 induce the recruitment of trans-activating TGA factors to a defense gene promoter in Arabidopsis. Plant Cell. 2003 Aug;15(8):1846-58. PMID:12897257
↑ Despres C, Chubak C, Rochon A, Clark R, Bethune T, Desveaux D, Fobert PR. The Arabidopsis NPR1 disease resistance protein is a novel cofactor that confers redox regulation of DNA binding activity to the basic domain/leucine zipper transcription factor TGA1. Plant Cell. 2003 Sep;15(9):2181-91. doi: 10.1105/tpc.012849. PMID:12953119 doi:http://dx.doi.org/10.1105/tpc.012849
↑ Shah J, Tsui F, Klessig DF. Characterization of a salicylic acid-insensitive mutant (sai1) of Arabidopsis thaliana, identified in a selective screen utilizing the SA-inducible expression of the tms2 gene. Mol Plant Microbe Interact. 1997 Jan;10(1):69-78. doi: 10.1094/MPMI.1997.10.1.69. PMID:9002272 doi:http://dx.doi.org/10.1094/MPMI.1997.10.1.69
↑ Cao H, Glazebrook J, Clarke JD, Volko S, Dong X. The Arabidopsis NPR1 gene that controls systemic acquired resistance encodes a novel protein containing ankyrin repeats. Cell. 1997 Jan 10;88(1):57-63. PMID:9019406
↑ Kumar S, Zavaliev R, Wu Q, Zhou Y, Cheng J, Dillard L, Powers J, Withers J, Zhao J, Guan Z, Borgnia MJ, Bartesaghi A, Dong X, Zhou P. Structural basis of NPR1 in activating plant immunity. Nature. 2022 May;605(7910):561-566. doi: 10.1038/s41586-022-04699-w. Epub 2022, May 11. PMID:35545668 doi:http://dx.doi.org/10.1038/s41586-022-04699-w

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7mk3"

Categories: Arabidopsis thaliana | Large Structures | Cheng J | Wu Q | Zhou P

@@ Line 3: / Line 3: @@
 <StructureSection load='7mk3' size='340' side='right'caption='[[7mk3]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7mk3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MK3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7mk3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MK3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 3.06&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[https://proteopedia.org/fgij/fg.htm?mol=7mk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mk3 OCA], [https://pdbe.org/7mk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mk3 RCSB], [https://www.ebi.ac.uk/pdbsum/7mk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mk3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/NPR1_ARATH NPR1_ARATH]] May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Key positive regulator of the SA-dependent signaling pathway that negatively regulates JA-dependent signaling pathway. Mediates the binding of TGA factors to the as-1 motif found in the pathogenesis-related PR-1 gene, leading to the transcriptional regulation of the gene defense. Controls the onset of systemic acquired resistance (SAR). Upon SAR induction, a biphasic change in cellular reduction potential occurs, resulting in reduction of the cytoplasmic oligomeric form to a monomeric form that accumulates in the nucleus and activates gene expression. Phosphorylated form is target of proteasome degradation.<ref>PMID:11607555</ref> <ref>PMID:12615947</ref> <ref>PMID:12837250</ref> <ref>PMID:12897257</ref> <ref>PMID:12953119</ref> <ref>PMID:9002272</ref> <ref>PMID:9019406</ref>
+[https://www.uniprot.org/uniprot/NPR1_ARATH NPR1_ARATH] May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Key positive regulator of the SA-dependent signaling pathway that negatively regulates JA-dependent signaling pathway. Mediates the binding of TGA factors to the as-1 motif found in the pathogenesis-related PR-1 gene, leading to the transcriptional regulation of the gene defense. Controls the onset of systemic acquired resistance (SAR). Upon SAR induction, a biphasic change in cellular reduction potential occurs, resulting in reduction of the cytoplasmic oligomeric form to a monomeric form that accumulates in the nucleus and activates gene expression. Phosphorylated form is target of proteasome degradation.<ref>PMID:11607555</ref> <ref>PMID:12615947</ref> <ref>PMID:12837250</ref> <ref>PMID:12897257</ref> <ref>PMID:12953119</ref> <ref>PMID:9002272</ref> <ref>PMID:9019406</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Cheng, J]]
+[[Category: Cheng J]]
-[[Category: Wu, Q]]
+[[Category: Wu Q]]
-[[Category: Zhou, P]]
+[[Category: Zhou P]]
-[[Category: Immune system]]
-[[Category: Npr1]]
-[[Category: Plant immunity]]
-[[Category: Plant protein]]
-[[Category: Sar]]

7mk3

From Proteopedia

Current revision

Crystal structure of NPR1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox