4mn8
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains== | |
| - | + | <StructureSection load='4mn8' size='340' side='right' caption='[[4mn8]], [[Resolution|resolution]] 3.06Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4mn8]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MN8 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mna|4mna]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FLS2, At5g46330, MPL12.13, MPL12.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), BAK1, ELG, SERK3, At4g33430, F17M5.190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mn8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mn8 RCSB], [http://www.ebi.ac.uk/pdbsum/4mn8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://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> [[http://www.uniprot.org/uniprot/BAK1_ARATH BAK1_ARATH]] Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1-BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) via its interaction with FLS2 and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR-independent cell-death pathway.<ref>PMID:17600708</ref> <ref>PMID:17583510</ref> <ref>PMID:18694562</ref> <ref>PMID:18667726</ref> <ref>PMID:19124768</ref> <ref>PMID:20018402</ref> <ref>PMID:20404519</ref> <ref>PMID:21350342</ref> | [[http://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> [[http://www.uniprot.org/uniprot/BAK1_ARATH BAK1_ARATH]] Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1-BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) via its interaction with FLS2 and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR-independent cell-death pathway.<ref>PMID:17600708</ref> <ref>PMID:17583510</ref> <ref>PMID:18694562</ref> <ref>PMID:18667726</ref> <ref>PMID:19124768</ref> <ref>PMID:20018402</ref> <ref>PMID:20404519</ref> <ref>PMID:21350342</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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arath]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
| - | [[Category: Chai, J | + | [[Category: Chai, J]] |
| - | [[Category: Han, Z | + | [[Category: Han, Z]] |
| - | [[Category: Sun, Y | + | [[Category: Sun, Y]] |
[[Category: Bak1]] | [[Category: Bak1]] | ||
[[Category: Flagellin]] | [[Category: Flagellin]] | ||
Revision as of 08:11, 25 December 2014
Crystal structure of flg22 in complex with the FLS2 and BAK1 ectodomains
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