4oh4

From Proteopedia

(Difference between revisions)

Revision as of 18:32, 4 August 2016

Crystal structure of BRI1 in complex with BKI1

Structural highlights

4oh4 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BRI1_ARATH] Receptor with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development, including expression of light- and stress-regulated genes, promotion of cell elongation, normal leaf and chloroplast senescence, and flowering. Binds brassinolide, and less effectively castasterone, but not 2,3,22,23-O-tetramethylbrassinolide or ecdysone. May be involved in a feedback regulation of brassinosteroid biosynthesis. Phosphorylates BRI1-associated receptor kinase 1 (BAK1), Transthyretin-Like protein (TTL) and SERK1 on 'Ser-299' and 'Thr-462' in vitro. May have a guanylyl cyclase activity.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] [BKI1_ARATH] Negative regulator of brassinosteroid signaling. When associated to the membrane, limits the interaction of BRI1 with BAK1 by binding to the kinase-inactive form of BRI1.^[7]

Publication Abstract from PubMed

Brassinosteroids (BRs) are essential steroid hormones that have crucial roles in plant growth and development. BRs are perceived by the cell-surface receptor-like kinase brassinosteroid insensitive 1 (BRI1). In the absence of BRs, the cytosolic kinase domain (KD) of BRI1 is inhibited by its auto-inhibitory carboxyl terminus, as well as by interacting with an inhibitor protein, BRI1 kinase inhibitor 1 (BKI1). How BR binding to the extracellular domain of BRI1 leads to activation of the KD and dissociation of BKI1 into the cytosol remains unclear. Here we report the crystal structure of BRI1 KD in complex with the interacting peptide derived from BKI1. We also provide biochemical evidence that BRI1-associated kinase 1 (BAK1) plays an essential role in initiating BR signaling. Steroid-dependent heterodimerization of BRI1 and BAK1 ectodomains brings their cytoplasmic KDs in the right orientation for competing with BKI1 and transphosphorylation.Cell Research advance online publication 21 October 2014; doi:10.1038/cr.2014.132.

Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1.,Wang J, Jiang J, Wang J, Chen L, Fan SL, Wu JW, Wang X, Wang ZX Cell Res. 2014 Oct 21. doi: 10.1038/cr.2014.132. PMID:25331450^[8]

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

References

↑ Noguchi T, Fujioka S, Choe S, Takatsuto S, Yoshida S, Yuan H, Feldmann KA, Tax FE. Brassinosteroid-insensitive dwarf mutants of Arabidopsis accumulate brassinosteroids. Plant Physiol. 1999 Nov;121(3):743-52. PMID:10557222
↑ Friedrichsen DM, Joazeiro CA, Li J, Hunter T, Chory J. Brassinosteroid-insensitive-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase. Plant Physiol. 2000 Aug;123(4):1247-56. PMID:10938344
↑ Belkhadir Y, Chory J. Brassinosteroid signaling: a paradigm for steroid hormone signaling from the cell surface. Science. 2006 Dec 1;314(5804):1410-1. PMID:17138891 doi:http://dx.doi.org/10.1126/science.1134040
↑ Kwezi L, Meier S, Mungur L, Ruzvidzo O, Irving H, Gehring C. The Arabidopsis thaliana brassinosteroid receptor (AtBRI1) contains a domain that functions as a guanylyl cyclase in vitro. PLoS One. 2007 May 23;2(5):e449. PMID:17520012 doi:http://dx.doi.org/10.1371/journal.pone.0000449
↑ 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
↑ 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
↑ Wang X, Chory J. Brassinosteroids regulate dissociation of BKI1, a negative regulator of BRI1 signaling, from the plasma membrane. Science. 2006 Aug 25;313(5790):1118-22. Epub 2006 Jul 20. PMID:16857903 doi:http://dx.doi.org/10.1126/science.1127593
↑ Wang J, Jiang J, Wang J, Chen L, Fan SL, Wu JW, Wang X, Wang ZX. Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1. Cell Res. 2014 Oct 21. doi: 10.1038/cr.2014.132. PMID:25331450 doi:http://dx.doi.org/10.1038/cr.2014.132

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/4oh4"

@@ Line 1: / Line 1: @@
 ==Crystal structure of BRI1 in complex with BKI1==
 <StructureSection load='4oh4' size='340' side='right' caption='[[4oh4]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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='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=4oh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oh4 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh4 PDBsum]</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=4oh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oh4 OCA], [http://pdbe.org/4oh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oh4 RCSB], [http://www.ebi.ac.uk/pdbsum/4oh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oh4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4oh4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4oh4

From Proteopedia

Revision as of 18:32, 4 August 2016

Crystal structure of BRI1 in complex with BKI1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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