4lsa: Difference between revisions

Revision as of 11:24, 14 December 2022

Crystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolide

Structural highlights

4lsa 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:	BLD, BMA, MAN, NAG
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]

Publication Abstract from PubMed

Brassinosteroids, which control plant growth and development, are sensed by the leucine-rich repeat (LRR) domain of the membrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1), but it is unknown how steroid binding at the cell surface activates the cytoplasmic kinase domain of the receptor. A family of somatic embryogenesis receptor kinases (SERKs) has been genetically implicated in mediating early brassinosteroid signaling events. We found a direct and steroid-dependent interaction between the BRI1 and SERK1 LRR domains by analysis of their complex crystal structure at 3.3 angstrom resolution. We show that the SERK1 LRR domain is involved in steroid sensing and, through receptor-co-receptor heteromerization, in the activation of the BRI1 signaling pathway. Our work reveals how known missense mutations in BRI1 and in SERKs modulate brassinosteroid signaling and the targeting mechanism of BRI1 receptor antagonists.

Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases.,Santiago J, Henzler C, Hothorn M Science. 2013 Aug 23;341(6148):889-92. doi: 10.1126/science.1242468. Epub 2013, Aug 8. PMID:23929946^[7]

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:https://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:https://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
↑ Santiago J, Henzler C, Hothorn M. Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases. Science. 2013 Aug 23;341(6148):889-92. doi: 10.1126/science.1242468. Epub 2013, Aug 8. PMID:23929946 doi:10.1126/science.1242468

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OCA

[1] 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

[2] 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

[3] 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:https://dx.doi.org/10.1126/science.1134040

[4] 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:https://dx.doi.org/10.1371/journal.pone.0000449

[5] 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

[6] 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

[7] Santiago J, Henzler C, Hothorn M. Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases. Science. 2013 Aug 23;341(6148):889-92. doi: 10.1126/science.1242468. Epub 2013, Aug 8. PMID:23929946 doi:10.1126/science.1242468

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[2]

[3]

[4]

[5]

[6]

[7]

@@ Line 1: / Line 1: @@
 ==Crystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolide==
-<StructureSection load='4lsa' size='340' side='right' caption='[[4lsa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='4lsa' size='340' side='right'caption='[[4lsa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4lsa]] is a 1 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=4LSA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LSA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4lsa]] is a 1 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=4LSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LSA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BLD:BRASSINOLIDE'>BLD</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLD:BRASSINOLIDE'>BLD</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3riz|3riz]], [[3rj0|3rj0]], [[4lsc|4lsc]], [[4lsx|4lsx]]</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=4lsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lsa OCA], [https://pdbe.org/4lsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lsa RCSB], [https://www.ebi.ac.uk/pdbsum/4lsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lsa ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At4g39400, BRI1, F23K16.30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=4lsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lsa OCA], [http://pdbe.org/4lsa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lsa RCSB], [http://www.ebi.ac.uk/pdbsum/4lsa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lsa ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BRI1_ARATH 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.<ref>PMID:10557222</ref> <ref>PMID:10938344</ref> <ref>PMID:17138891</ref> <ref>PMID:17520012</ref> <ref>PMID:18694562</ref> <ref>PMID:19124768</ref>
+[https://www.uniprot.org/uniprot/BRI1_ARATH 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.<ref>PMID:10557222</ref> <ref>PMID:10938344</ref> <ref>PMID:17138891</ref> <ref>PMID:17520012</ref> <ref>PMID:18694562</ref> <ref>PMID:19124768</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Henzler, C]]
+[[Category: Large Structures]]
-[[Category: Hothorn, M]]
+[[Category: Henzler C]]
-[[Category: Santiago, J]]
+[[Category: Hothorn M]]
-[[Category: Brassinosteroid binding]]
+[[Category: Santiago J]]
-[[Category: Lrr-domain]]
-[[Category: Membrane receptor]]
-[[Category: N-glycosylation]]
-[[Category: Protein binding]]
-[[Category: Steroid binding protein]]

4lsa: Difference between revisions

Revision as of 11:24, 14 December 2022

Crystal structure of BRI1 sud1 (Gly643Glu) bound to brassinolide

Structural highlights

Function

Publication Abstract from PubMed

References

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