4c6r: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c6r]] is a 4 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=4C6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6R FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c6r]] is a 4 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=4C6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6R 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=4c6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6r OCA], [https://pdbe.org/4c6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6r RCSB], [https://www.ebi.ac.uk/pdbsum/4c6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6r ProSAT]</span></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]] 2.05Å</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=4c6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6r OCA], [https://pdbe.org/4c6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6r RCSB], [https://www.ebi.ac.uk/pdbsum/4c6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RPS4_ARATH RPS4_ARATH] Disease resistance (R) protein that specifically recognizes the AvrRps4 type III effector avirulence protein from P.syringae (PubMed:10571887, PubMed:15469494, PubMed:19519800). Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein (PubMed:10571887, PubMed:15469494, PubMed:19519800). That triggers a defense system including the hypersensitive response, which restricts the pathogen growth (PubMed:10571887, PubMed:15469494, PubMed:19519800). Probably acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439792, PubMed:31439793). The combined presence of both regular and alternative RPS4 transcripts with truncated open reading frames (ORFs) is necessary for function (PubMed:17951452). RPS4 function is regulated at multiple levels, including gene expression, alternative splicing, and protein stability (PubMed:17951452). When over-expressed, confers temperature-conditioned EDS1-dependent auto-immunity (PubMed:24146667). Heterodimerization with RRS1 is required to form a functional complex to recognize AvrRps4 and PopP2 (PubMed:24744375). Abscisic acid deficiency enhances nuclear accumulation of RPS4 and its cell death-inducing activity (PubMed:22454454).<ref>PMID:10571887</ref> <ref>PMID:15469494</ref> <ref>PMID:17951452</ref> <ref>PMID:19519800</ref> <ref>PMID:22454454</ref> <ref>PMID:24146667</ref> <ref>PMID:24744375</ref> <ref>PMID:31439792</ref> <ref>PMID:31439793</ref> <ref>PMID:17951452</ref> <ref>PMID:19519800</ref> | |||
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== Publication Abstract from PubMed == | |||
Cytoplasmic plant immune receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the immune receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate. Crystal structures of the N-terminal Toll-interleukin-1 receptor/resistance (TIR) domains of RPS4 and RRS1, individually and as a heterodimeric complex (respectively at 2.05, 1.75, and 2.65 angstrom resolution), reveal a conserved TIR/TIR interaction interface. We show that TIR domain heterodimerization is required to form a functional RRS1/RPS4 effector recognition complex. The RPS4 TIR domain activates effector-independent defense, which is inhibited by the RRS1 TIR domain through the heterodimerization interface. Thus, RPS4 and RRS1 function as a receptor complex in which the two components play distinct roles in recognition and signaling. | |||
Structural basis for assembly and function of a heterodimeric plant immune receptor.,Williams SJ, Sohn KH, Wan L, Bernoux M, Sarris PF, Segonzac C, Ve T, Ma Y, Saucet SB, Ericsson DJ, Casey LW, Lonhienne T, Winzor DJ, Zhang X, Coerdt A, Parker JE, Dodds PN, Kobe B, Jones JD Science. 2014 Apr 18;344(6181):299-303. doi: 10.1126/science.1247357. PMID:24744375<ref>PMID:24744375</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
<references/> | <references/> | ||