4mn8: Difference between revisions

Latest revision as of 14:43, 8 November 2023

Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains

Structural highlights

4mn8 is a 3 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 3.062Å
Ligands:	NAG, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FLS2_ARATH Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of flagellin (flg22), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Flagellin-binding to the receptor is the first step to initiate the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6), resulting in enhanced resistance against pathogens. Binding to the effector AvrPto1 from Pseudomonas syringae blocks the downstream plant immune response.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Flagellin perception in Arabidopsis is through recognition of its highly conserved N-terminal epitope (flg22) by flagellin-sensitive 2 (FLS2). Flg22 binding induces FLS2 heteromerization with BRASSINOSTEROID INSENSITIVE 1-associated kinase 1 (BAK1) and their reciprocal activation followed by plant immunity. Here, we report the crystal structure of FLS2 and BAK1 ectodomains complexed with flg22 at 3.06 angstroms. A conserved and a nonconserved site from the inner surface of the FLS2 solenoid recognize the C- and N-terminal segment of flg22, respectively, without oligomerization or conformational changes in the FLS2 ectodomain. Besides directly interacting with FLS2, BAK1 acts as a co-receptor by recognizing the C terminus of the FLS2-bound flg22. Our data reveal the molecular mechanisms underlying FLS2-BAK1 complex recognition of flg22 and provide insight into the immune receptor complex activation.

Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.,Sun Y, Li L, Macho AP, Han Z, Hu Z, Zipfel C, Zhou JM, Chai J Science. 2013 Nov 1;342(6158):624-8. doi: 10.1126/science.1243825. Epub 2013 Oct , 10. PMID:24114786^[7]

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

References

↑ Gomez-Gomez L, Boller T. FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis. Mol Cell. 2000 Jun;5(6):1003-11. PMID:10911994
↑ Gomez-Gomez L, Bauer Z, Boller T. Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis. Plant Cell. 2001 May;13(5):1155-63. PMID:11340188
↑ Asai T, Tena G, Plotnikova J, Willmann MR, Chiu WL, Gomez-Gomez L, Boller T, Ausubel FM, Sheen J. MAP kinase signalling cascade in Arabidopsis innate immunity. Nature. 2002 Feb 28;415(6875):977-83. PMID:11875555 doi:https://dx.doi.org/10.1038/415977a
↑ Zipfel C, Robatzek S, Navarro L, Oakeley EJ, Jones JD, Felix G, Boller T. Bacterial disease resistance in Arabidopsis through flagellin perception. Nature. 2004 Apr 15;428(6984):764-7. PMID:15085136 doi:https://dx.doi.org/10.1038/nature02485
↑ Gohre V, Spallek T, Haweker H, Mersmann S, Mentzel T, Boller T, de Torres M, Mansfield JW, Robatzek S. Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB. Curr Biol. 2008 Dec 9;18(23):1824-32. doi: 10.1016/j.cub.2008.10.063. PMID:19062288 doi:https://dx.doi.org/10.1016/j.cub.2008.10.063
↑ Chinchilla D, Bauer Z, Regenass M, Boller T, Felix G. The Arabidopsis receptor kinase FLS2 binds flg22 and determines the specificity of flagellin perception. Plant Cell. 2006 Feb;18(2):465-76. Epub 2005 Dec 23. PMID:16377758 doi:https://dx.doi.org/10.1105/tpc.105.036574
↑ Sun Y, Li L, Macho AP, Han Z, Hu Z, Zipfel C, Zhou JM, Chai J. Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex. Science. 2013 Nov 1;342(6158):624-8. doi: 10.1126/science.1243825. Epub 2013 Oct , 10. PMID:24114786 doi:https://dx.doi.org/10.1126/science.1243825

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OCA

[1] Gomez-Gomez L, Boller T. FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis. Mol Cell. 2000 Jun;5(6):1003-11. PMID:10911994

[2] Gomez-Gomez L, Bauer Z, Boller T. Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis. Plant Cell. 2001 May;13(5):1155-63. PMID:11340188

[3] Asai T, Tena G, Plotnikova J, Willmann MR, Chiu WL, Gomez-Gomez L, Boller T, Ausubel FM, Sheen J. MAP kinase signalling cascade in Arabidopsis innate immunity. Nature. 2002 Feb 28;415(6875):977-83. PMID:11875555 doi:https://dx.doi.org/10.1038/415977a

[4] Zipfel C, Robatzek S, Navarro L, Oakeley EJ, Jones JD, Felix G, Boller T. Bacterial disease resistance in Arabidopsis through flagellin perception. Nature. 2004 Apr 15;428(6984):764-7. PMID:15085136 doi:https://dx.doi.org/10.1038/nature02485

[5] Gohre V, Spallek T, Haweker H, Mersmann S, Mentzel T, Boller T, de Torres M, Mansfield JW, Robatzek S. Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB. Curr Biol. 2008 Dec 9;18(23):1824-32. doi: 10.1016/j.cub.2008.10.063. PMID:19062288 doi:https://dx.doi.org/10.1016/j.cub.2008.10.063

[6] Chinchilla D, Bauer Z, Regenass M, Boller T, Felix G. The Arabidopsis receptor kinase FLS2 binds flg22 and determines the specificity of flagellin perception. Plant Cell. 2006 Feb;18(2):465-76. Epub 2005 Dec 23. PMID:16377758 doi:https://dx.doi.org/10.1105/tpc.105.036574

[7] Sun Y, Li L, Macho AP, Han Z, Hu Z, Zipfel C, Zhou JM, Chai J. Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex. Science. 2013 Nov 1;342(6158):624-8. doi: 10.1126/science.1243825. Epub 2013 Oct , 10. PMID:24114786 doi:https://dx.doi.org/10.1126/science.1243825

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4mn8 is ON HOLD
+==Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains==
+<StructureSection load='4mn8' size='340' side='right'caption='[[4mn8]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4mn8]] is a 3 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=4MN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MN8 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.062&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4mn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mn8 OCA], [https://pdbe.org/4mn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mn8 RCSB], [https://www.ebi.ac.uk/pdbsum/4mn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mn8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FLS2_ARATH FLS2_ARATH] Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of flagellin (flg22), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Flagellin-binding to the receptor is the first step to initiate the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6), resulting in enhanced resistance against pathogens. Binding to the effector AvrPto1 from Pseudomonas syringae blocks the downstream plant immune response.<ref>PMID:10911994</ref> <ref>PMID:11340188</ref> <ref>PMID:11875555</ref> <ref>PMID:15085136</ref> <ref>PMID:19062288</ref> <ref>PMID:16377758</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Flagellin perception in Arabidopsis is through recognition of its highly conserved N-terminal epitope (flg22) by flagellin-sensitive 2 (FLS2). Flg22 binding induces FLS2 heteromerization with BRASSINOSTEROID INSENSITIVE 1-associated kinase 1 (BAK1) and their reciprocal activation followed by plant immunity. Here, we report the crystal structure of FLS2 and BAK1 ectodomains complexed with flg22 at 3.06 angstroms. A conserved and a nonconserved site from the inner surface of the FLS2 solenoid recognize the C- and N-terminal segment of flg22, respectively, without oligomerization or conformational changes in the FLS2 ectodomain. Besides directly interacting with FLS2, BAK1 acts as a co-receptor by recognizing the C terminus of the FLS2-bound flg22. Our data reveal the molecular mechanisms underlying FLS2-BAK1 complex recognition of flg22 and provide insight into the immune receptor complex activation.
-Authors: Chai jijie , Sun yadong, Han zhifu
+Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex.,Sun Y, Li L, Macho AP, Han Z, Hu Z, Zipfel C, Zhou JM, Chai J Science. 2013 Nov 1;342(6158):624-8. doi: 10.1126/science.1243825. Epub 2013 Oct , 10. PMID:24114786<ref>PMID:24114786</ref>
-Description: Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4mn8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Chai J]]
+[[Category: Han Z]]
+[[Category: Sun Y]]

4mn8: Difference between revisions

Latest revision as of 14:43, 8 November 2023

Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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