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{{STRUCTURE_3uim|  PDB=3uim  |  SCENE=  }}
==Structural basis for the impact of phosphorylation on plant receptor-like kinase BAK1 activation==
===Structural basis for the impact of phosphorylation on plant receptor-like kinase BAK1 activation===
<StructureSection load='3uim' size='340' side='right' caption='[[3uim]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 
== Structural highlights ==
==Function==
<table><tr><td colspan='2'>[[3uim]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UIM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UIM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</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=3uim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uim OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uim RCSB], [http://www.ebi.ac.uk/pdbsum/3uim PDBsum]</span></td></tr>
</table>
== Function ==
[[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/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>   
 
== References ==
==About this Structure==
<references/>
[[3uim]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UIM OCA].
__TOC__
 
</StructureSection>
==Reference==
<ref group="xtra">PMID:022547027</ref><references group="xtra"/><references/>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Lou, Z Y.]]
[[Category: Lou, Z Y]]
[[Category: Ma, Y Y.]]
[[Category: Ma, Y Y]]
[[Category: Yan, L M.]]
[[Category: Yan, L M]]
[[Category: Kinase]]
[[Category: Kinase]]
[[Category: Protein kinase]]
[[Category: Protein kinase]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 20:07, 25 December 2014

Structural basis for the impact of phosphorylation on plant receptor-like kinase BAK1 activationStructural basis for the impact of phosphorylation on plant receptor-like kinase BAK1 activation

Structural highlights

3uim is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:,
Gene:BAK1 (Arabidopsis thaliana)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[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.[1] [2] [3] [4] [5] [6] [7] [8]

References

  1. ↑ He K, Gou X, Yuan T, Lin H, Asami T, Yoshida S, Russell SD, Li J. BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways. Curr Biol. 2007 Jul 3;17(13):1109-15. PMID:17600708 doi:10.1016/j.cub.2007.05.036
  2. ↑ Kemmerling B, Schwedt A, Rodriguez P, Mazzotta S, Frank M, Qamar SA, Mengiste T, Betsuyaku S, Parker JE, Mussig C, Thomma BP, Albrecht C, de Vries SC, Hirt H, Nurnberger T. The BRI1-associated kinase 1, BAK1, has a brassinolide-independent role in plant cell-death control. Curr Biol. 2007 Jul 3;17(13):1116-22. Epub 2007 Jun 21. PMID:17583510 doi:S0960-9822(07)01470-4
  3. ↑ Wang X, Kota U, He K, Blackburn K, Li J, Goshe MB, Huber SC, Clouse SD. Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling. Dev Cell. 2008 Aug;15(2):220-35. doi: 10.1016/j.devcel.2008.06.011. PMID:18694562 doi:10.1016/j.devcel.2008.06.011
  4. ↑ Albrecht C, Russinova E, Kemmerling B, Kwaaitaal M, de Vries SC. Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve brassinosteroid-dependent and -independent signaling pathways. Plant Physiol. 2008 Sep;148(1):611-9. doi: 10.1104/pp.108.123216. Epub 2008 Jul, 30. PMID:18667726 doi:10.1104/pp.108.123216
  5. ↑ Oh MH, Wang X, Kota U, Goshe MB, Clouse SD, Huber SC. Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis. Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):658-63. Epub 2009 Jan 5. PMID:19124768 doi:0810249106
  6. ↑ Postel S, Kufner I, Beuter C, Mazzotta S, Schwedt A, Borlotti A, Halter T, Kemmerling B, Nurnberger T. The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity. Eur J Cell Biol. 2010 Feb-Mar;89(2-3):169-74. doi: 10.1016/j.ejcb.2009.11.001., Epub 2009 Dec 16. PMID:20018402 doi:10.1016/j.ejcb.2009.11.001
  7. ↑ Lu D, Wu S, He P, Shan L. Phosphorylation of receptor-like cytoplasmic kinases by bacterial flagellin. Plant Signal Behav. 2010 May 9;5(5). PMID:20404519
  8. ↑ Oh MH, Wu X, Clouse SD, Huber SC. Functional importance of BAK1 tyrosine phosphorylation in vivo. Plant Signal Behav. 2011 Mar;6(3):400-5. Epub 2011 Mar 1. PMID:21350342

3uim, resolution 2.20Å

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